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Database: PDB
Entry: 5VEU
LinkDB: 5VEU
Original site: 5VEU 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 05-APR-17   5VEU              
TITLE     HUMAN CYTOCHROME P450 3A5 (CYP3A5)                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME P450 3A5;                                       
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;                           
COMPND   4 FRAGMENT: UNP RESIDUES 24-497;                                       
COMPND   5 SYNONYM: CYPIIIA5,CYTOCHROME P450 HLP2,CYTOCHROME P450-PCN3;         
COMPND   6 EC: 1.14.14.1;                                                       
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CYP3A5;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: DH-5A;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCWORI                                    
KEYWDS    INHIBITOR, COMPLEX, CYTOCHROME P450, RITONAVIR, CYP3A5,               
KEYWDS   2 OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.-H.HSU,E.F.JOHNSON                                                  
REVDAT   4   01-JAN-20 5VEU    1       REMARK                                   
REVDAT   3   10-JAN-18 5VEU    1       REMARK                                   
REVDAT   2   13-DEC-17 5VEU    1       JRNL                                     
REVDAT   1   15-NOV-17 5VEU    0                                                
JRNL        AUTH   M.H.HSU,U.SAVAS,E.F.JOHNSON                                  
JRNL        TITL   THE X-RAY CRYSTAL STRUCTURE OF THE HUMAN MONO-OXYGENASE      
JRNL        TITL 2 CYTOCHROME P450 3A5-RITONAVIR COMPLEX REVEALS ACTIVE SITE    
JRNL        TITL 3 DIFFERENCES BETWEEN P450S 3A4 AND 3A5.                       
JRNL        REF    MOL. PHARMACOL.               V.  93    14 2018              
JRNL        REFN                   ESSN 1521-0111                               
JRNL        PMID   29093019                                                     
JRNL        DOI    10.1124/MOL.117.109744                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.91 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.91                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.16                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.270                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 152082                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.216                           
REMARK   3   R VALUE            (WORKING SET) : 0.214                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.960                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7549                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 39.1588 -  9.0056    0.99     5081   255  0.1734 0.2113        
REMARK   3     2  9.0056 -  7.1623    0.99     4944   243  0.1642 0.1844        
REMARK   3     3  7.1623 -  6.2611    1.00     4952   221  0.1988 0.2346        
REMARK   3     4  6.2611 -  5.6905    1.00     4873   241  0.2072 0.2450        
REMARK   3     5  5.6905 -  5.2837    1.00     4857   276  0.1981 0.2122        
REMARK   3     6  5.2837 -  4.9728    1.00     4822   253  0.1935 0.2427        
REMARK   3     7  4.9728 -  4.7242    1.00     4882   251  0.1893 0.2439        
REMARK   3     8  4.7242 -  4.5189    1.00     4841   225  0.1989 0.2396        
REMARK   3     9  4.5189 -  4.3451    1.00     4869   251  0.1930 0.2348        
REMARK   3    10  4.3451 -  4.1954    1.00     4840   240  0.2022 0.2549        
REMARK   3    11  4.1954 -  4.0643    1.00     4839   228  0.2050 0.2310        
REMARK   3    12  4.0643 -  3.9483    1.00     4833   249  0.2181 0.2557        
REMARK   3    13  3.9483 -  3.8444    1.00     4772   265  0.2215 0.2801        
REMARK   3    14  3.8444 -  3.7507    1.00     4803   243  0.2223 0.2672        
REMARK   3    15  3.7507 -  3.6655    1.00     4800   265  0.2294 0.2715        
REMARK   3    16  3.6655 -  3.5875    1.00     4823   244  0.2361 0.2683        
REMARK   3    17  3.5875 -  3.5158    1.00     4802   248  0.2441 0.2897        
REMARK   3    18  3.5158 -  3.4495    1.00     4786   245  0.2455 0.3082        
REMARK   3    19  3.4495 -  3.3880    1.00     4754   288  0.2516 0.3091        
REMARK   3    20  3.3880 -  3.3306    1.00     4814   254  0.2597 0.3110        
REMARK   3    21  3.3306 -  3.2769    1.00     4771   268  0.2653 0.3012        
REMARK   3    22  3.2769 -  3.2265    1.00     4765   250  0.2664 0.3173        
REMARK   3    23  3.2265 -  3.1790    1.00     4765   260  0.2631 0.3332        
REMARK   3    24  3.1790 -  3.1343    1.00     4783   255  0.2642 0.3344        
REMARK   3    25  3.1343 -  3.0919    1.00     4802   257  0.2698 0.3332        
REMARK   3    26  3.0919 -  3.0518    1.00     4745   252  0.2663 0.3062        
REMARK   3    27  3.0518 -  3.0137    1.00     4760   271  0.2686 0.3433        
REMARK   3    28  3.0137 -  2.9774    1.00     4813   251  0.2841 0.3480        
REMARK   3    29  2.9774 -  2.9428    1.00     4794   268  0.2885 0.3325        
REMARK   3    30  2.9428 -  2.9097    0.95     4548   232  0.3103 0.3781        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.420            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.980           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 70.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005          45903                                  
REMARK   3   ANGLE     :  1.066          62309                                  
REMARK   3   CHIRALITY :  0.067           6945                                  
REMARK   3   PLANARITY :  0.005           7917                                  
REMARK   3   DIHEDRAL  : 11.730          17549                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5VEU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000227319.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.106965                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 152197                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.910                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.160                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.91                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.96                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3NXU                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, PEG 300, ADA, ZINC SULFATE,    
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 297K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       74.49400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      117.44050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       99.19200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      117.44050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       74.49400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       99.19200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12                   
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 7                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 8                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 9                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 10                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 11                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 12                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    22                                                      
REMARK 465     ALA A    23                                                      
REMARK 465     LEU A    24                                                      
REMARK 465     TYR A    25                                                      
REMARK 465     GLY A    26                                                      
REMARK 465     LYS A   282                                                      
REMARK 465     GLU A   283                                                      
REMARK 465     THR A   284                                                      
REMARK 465     GLU A   285                                                      
REMARK 465     SER A   286                                                      
REMARK 465     HIS A   287                                                      
REMARK 465     LYS A   288                                                      
REMARK 465     ASP A   496                                                      
REMARK 465     GLY A   497                                                      
REMARK 465     HIS A   498                                                      
REMARK 465     HIS A   499                                                      
REMARK 465     HIS A   500                                                      
REMARK 465     HIS A   501                                                      
REMARK 465     MET B    22                                                      
REMARK 465     ALA B    23                                                      
REMARK 465     LEU B    24                                                      
REMARK 465     TYR B    25                                                      
REMARK 465     GLY B    26                                                      
REMARK 465     LYS B   282                                                      
REMARK 465     GLU B   283                                                      
REMARK 465     THR B   284                                                      
REMARK 465     GLU B   285                                                      
REMARK 465     SER B   286                                                      
REMARK 465     HIS B   287                                                      
REMARK 465     LYS B   288                                                      
REMARK 465     LYS B   421                                                      
REMARK 465     LYS B   422                                                      
REMARK 465     LYS B   423                                                      
REMARK 465     ASP B   424                                                      
REMARK 465     ASP B   496                                                      
REMARK 465     GLY B   497                                                      
REMARK 465     HIS B   498                                                      
REMARK 465     HIS B   499                                                      
REMARK 465     HIS B   500                                                      
REMARK 465     HIS B   501                                                      
REMARK 465     MET C    22                                                      
REMARK 465     ALA C    23                                                      
REMARK 465     LEU C    24                                                      
REMARK 465     TYR C    25                                                      
REMARK 465     GLY C    26                                                      
REMARK 465     ASP C   496                                                      
REMARK 465     GLY C   497                                                      
REMARK 465     HIS C   498                                                      
REMARK 465     HIS C   499                                                      
REMARK 465     HIS C   500                                                      
REMARK 465     HIS C   501                                                      
REMARK 465     MET D    22                                                      
REMARK 465     ALA D    23                                                      
REMARK 465     LEU D    24                                                      
REMARK 465     TYR D    25                                                      
REMARK 465     GLY D    26                                                      
REMARK 465     LYS D   282                                                      
REMARK 465     GLU D   283                                                      
REMARK 465     THR D   284                                                      
REMARK 465     GLU D   285                                                      
REMARK 465     SER D   286                                                      
REMARK 465     HIS D   287                                                      
REMARK 465     LYS D   288                                                      
REMARK 465     LYS D   421                                                      
REMARK 465     LYS D   422                                                      
REMARK 465     LYS D   423                                                      
REMARK 465     ASP D   496                                                      
REMARK 465     GLY D   497                                                      
REMARK 465     HIS D   498                                                      
REMARK 465     HIS D   499                                                      
REMARK 465     HIS D   500                                                      
REMARK 465     HIS D   501                                                      
REMARK 465     MET E    22                                                      
REMARK 465     ALA E    23                                                      
REMARK 465     LEU E    24                                                      
REMARK 465     TYR E    25                                                      
REMARK 465     GLY E    26                                                      
REMARK 465     LYS E   166                                                      
REMARK 465     GLY E   167                                                      
REMARK 465     LYS E   168                                                      
REMARK 465     ASP E   263                                                      
REMARK 465     LYS E   264                                                      
REMARK 465     GLN E   265                                                      
REMARK 465     LYS E   266                                                      
REMARK 465     HIS E   267                                                      
REMARK 465     ARG E   268                                                      
REMARK 465     ASN E   280                                                      
REMARK 465     SER E   281                                                      
REMARK 465     LYS E   282                                                      
REMARK 465     GLU E   283                                                      
REMARK 465     THR E   284                                                      
REMARK 465     GLU E   285                                                      
REMARK 465     SER E   286                                                      
REMARK 465     HIS E   287                                                      
REMARK 465     LYS E   288                                                      
REMARK 465     LYS E   421                                                      
REMARK 465     LYS E   422                                                      
REMARK 465     LYS E   423                                                      
REMARK 465     ASP E   424                                                      
REMARK 465     SER E   425                                                      
REMARK 465     LYS E   491                                                      
REMARK 465     VAL E   492                                                      
REMARK 465     ASP E   493                                                      
REMARK 465     SER E   494                                                      
REMARK 465     ARG E   495                                                      
REMARK 465     ASP E   496                                                      
REMARK 465     GLY E   497                                                      
REMARK 465     HIS E   498                                                      
REMARK 465     HIS E   499                                                      
REMARK 465     HIS E   500                                                      
REMARK 465     HIS E   501                                                      
REMARK 465     MET F    22                                                      
REMARK 465     ALA F    23                                                      
REMARK 465     LEU F    24                                                      
REMARK 465     TYR F    25                                                      
REMARK 465     GLY F    26                                                      
REMARK 465     THR F    27                                                      
REMARK 465     ARG F    28                                                      
REMARK 465     LYS F   282                                                      
REMARK 465     GLU F   283                                                      
REMARK 465     THR F   284                                                      
REMARK 465     GLU F   285                                                      
REMARK 465     SER F   286                                                      
REMARK 465     HIS F   287                                                      
REMARK 465     LYS F   288                                                      
REMARK 465     LYS F   421                                                      
REMARK 465     LYS F   422                                                      
REMARK 465     LYS F   423                                                      
REMARK 465     ASP F   424                                                      
REMARK 465     ASP F   496                                                      
REMARK 465     GLY F   497                                                      
REMARK 465     HIS F   498                                                      
REMARK 465     HIS F   499                                                      
REMARK 465     HIS F   500                                                      
REMARK 465     HIS F   501                                                      
REMARK 465     MET G    22                                                      
REMARK 465     ALA G    23                                                      
REMARK 465     LEU G    24                                                      
REMARK 465     TYR G    25                                                      
REMARK 465     GLY G    26                                                      
REMARK 465     GLN G   265                                                      
REMARK 465     LYS G   266                                                      
REMARK 465     HIS G   267                                                      
REMARK 465     LYS G   282                                                      
REMARK 465     GLU G   283                                                      
REMARK 465     THR G   284                                                      
REMARK 465     GLU G   285                                                      
REMARK 465     SER G   286                                                      
REMARK 465     HIS G   287                                                      
REMARK 465     LYS G   288                                                      
REMARK 465     LYS G   421                                                      
REMARK 465     LYS G   422                                                      
REMARK 465     LYS G   423                                                      
REMARK 465     ASP G   424                                                      
REMARK 465     ASP G   496                                                      
REMARK 465     GLY G   497                                                      
REMARK 465     HIS G   498                                                      
REMARK 465     HIS G   499                                                      
REMARK 465     HIS G   500                                                      
REMARK 465     HIS G   501                                                      
REMARK 465     MET H    22                                                      
REMARK 465     ALA H    23                                                      
REMARK 465     LEU H    24                                                      
REMARK 465     TYR H    25                                                      
REMARK 465     GLY H    26                                                      
REMARK 465     LYS H   282                                                      
REMARK 465     GLU H   283                                                      
REMARK 465     THR H   284                                                      
REMARK 465     GLU H   285                                                      
REMARK 465     SER H   286                                                      
REMARK 465     HIS H   287                                                      
REMARK 465     LYS H   288                                                      
REMARK 465     LYS H   421                                                      
REMARK 465     LYS H   422                                                      
REMARK 465     LYS H   423                                                      
REMARK 465     ASP H   496                                                      
REMARK 465     GLY H   497                                                      
REMARK 465     HIS H   498                                                      
REMARK 465     HIS H   499                                                      
REMARK 465     HIS H   500                                                      
REMARK 465     HIS H   501                                                      
REMARK 465     MET I    22                                                      
REMARK 465     ALA I    23                                                      
REMARK 465     LEU I    24                                                      
REMARK 465     TYR I    25                                                      
REMARK 465     GLY I    26                                                      
REMARK 465     LYS I   421                                                      
REMARK 465     LYS I   422                                                      
REMARK 465     LYS I   423                                                      
REMARK 465     ASP I   424                                                      
REMARK 465     SER I   425                                                      
REMARK 465     ASP I   496                                                      
REMARK 465     GLY I   497                                                      
REMARK 465     HIS I   498                                                      
REMARK 465     HIS I   499                                                      
REMARK 465     HIS I   500                                                      
REMARK 465     HIS I   501                                                      
REMARK 465     MET J    22                                                      
REMARK 465     ALA J    23                                                      
REMARK 465     LEU J    24                                                      
REMARK 465     TYR J    25                                                      
REMARK 465     GLY J    26                                                      
REMARK 465     LYS J   282                                                      
REMARK 465     GLU J   283                                                      
REMARK 465     THR J   284                                                      
REMARK 465     GLU J   285                                                      
REMARK 465     SER J   286                                                      
REMARK 465     HIS J   287                                                      
REMARK 465     LYS J   288                                                      
REMARK 465     LYS J   421                                                      
REMARK 465     LYS J   422                                                      
REMARK 465     LYS J   423                                                      
REMARK 465     ASP J   424                                                      
REMARK 465     ASP J   496                                                      
REMARK 465     GLY J   497                                                      
REMARK 465     HIS J   498                                                      
REMARK 465     HIS J   499                                                      
REMARK 465     HIS J   500                                                      
REMARK 465     HIS J   501                                                      
REMARK 465     MET K    22                                                      
REMARK 465     ALA K    23                                                      
REMARK 465     LEU K    24                                                      
REMARK 465     TYR K    25                                                      
REMARK 465     GLY K    26                                                      
REMARK 465     SER K   281                                                      
REMARK 465     LYS K   282                                                      
REMARK 465     GLU K   283                                                      
REMARK 465     THR K   284                                                      
REMARK 465     GLU K   285                                                      
REMARK 465     SER K   286                                                      
REMARK 465     HIS K   287                                                      
REMARK 465     LYS K   288                                                      
REMARK 465     LYS K   421                                                      
REMARK 465     LYS K   422                                                      
REMARK 465     LYS K   423                                                      
REMARK 465     ASP K   496                                                      
REMARK 465     GLY K   497                                                      
REMARK 465     HIS K   498                                                      
REMARK 465     HIS K   499                                                      
REMARK 465     HIS K   500                                                      
REMARK 465     HIS K   501                                                      
REMARK 465     MET L    22                                                      
REMARK 465     ALA L    23                                                      
REMARK 465     LEU L    24                                                      
REMARK 465     TYR L    25                                                      
REMARK 465     GLY L    26                                                      
REMARK 465     ASP L   263                                                      
REMARK 465     LYS L   264                                                      
REMARK 465     GLN L   265                                                      
REMARK 465     LYS L   266                                                      
REMARK 465     HIS L   267                                                      
REMARK 465     ARG L   268                                                      
REMARK 465     LEU L   269                                                      
REMARK 465     ASP L   270                                                      
REMARK 465     LYS L   282                                                      
REMARK 465     GLU L   283                                                      
REMARK 465     THR L   284                                                      
REMARK 465     GLU L   285                                                      
REMARK 465     SER L   286                                                      
REMARK 465     HIS L   287                                                      
REMARK 465     LYS L   288                                                      
REMARK 465     LYS L   421                                                      
REMARK 465     LYS L   422                                                      
REMARK 465     LYS L   423                                                      
REMARK 465     ASP L   424                                                      
REMARK 465     SER L   425                                                      
REMARK 465     ARG L   495                                                      
REMARK 465     ASP L   496                                                      
REMARK 465     GLY L   497                                                      
REMARK 465     HIS L   498                                                      
REMARK 465     HIS L   499                                                      
REMARK 465     HIS L   500                                                      
REMARK 465     HIS L   501                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU D   410     NH2  ARG D   415              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A  95      -64.22   -124.17                                   
REMARK 500    VAL A 101      -63.37   -130.13                                   
REMARK 500    ARG A 105      -71.37    -78.69                                   
REMARK 500    ASP A 123     -133.39     58.63                                   
REMARK 500    PRO A 135        3.29    -66.37                                   
REMARK 500    GLN A 200       59.62   -116.58                                   
REMARK 500    ILE A 383      -66.77    -98.15                                   
REMARK 500    GLU A 410       73.80     54.13                                   
REMARK 500    GLU B  97       34.95    -95.75                                   
REMARK 500    PHE B 102       61.06   -106.73                                   
REMARK 500    MET B 114        6.10    -69.57                                   
REMARK 500    ASP B 123     -138.84     59.65                                   
REMARK 500    GLN B 200       58.42   -119.52                                   
REMARK 500    ASP B 270     -164.27   -120.64                                   
REMARK 500    ILE B 383     -150.73    -91.81                                   
REMARK 500    PRO B 397       83.45    -68.26                                   
REMARK 500    GLU B 410       74.04     52.51                                   
REMARK 500    PHE B 419       44.12    -96.63                                   
REMARK 500    CYS B 467     -169.03   -122.01                                   
REMARK 500    VAL C  95      -65.48   -120.54                                   
REMARK 500    PHE C 102       67.58   -106.49                                   
REMARK 500    ASP C 123     -133.85     58.74                                   
REMARK 500    GLN C 200       52.95   -114.94                                   
REMARK 500    ARG C 260       36.89    -84.25                                   
REMARK 500    GLN C 265       15.77     58.97                                   
REMARK 500    LYS C 266       38.06    -85.53                                   
REMARK 500    ARG C 268       -4.15     63.22                                   
REMARK 500    GLU C 283       60.28     66.35                                   
REMARK 500    ASP C 424      -75.33    -54.29                                   
REMARK 500    GLU D  97       40.67    -97.89                                   
REMARK 500    VAL D 101      -50.20   -125.54                                   
REMARK 500    PHE D 102       66.25   -107.21                                   
REMARK 500    ASP D 123     -132.77     60.39                                   
REMARK 500    ASP D 270     -164.59   -108.25                                   
REMARK 500    PRO D 397       84.82    -68.05                                   
REMARK 500    GLU D 410       74.11     56.19                                   
REMARK 500    PRO D 428        1.07    -69.99                                   
REMARK 500    ASN D 461      -30.00   -131.07                                   
REMARK 500    CYS D 467     -166.05   -128.54                                   
REMARK 500    VAL E  95      -74.70   -114.76                                   
REMARK 500    LYS E  96      -70.71    -55.78                                   
REMARK 500    GLU E  97       30.83    -86.84                                   
REMARK 500    VAL E 101      -58.87   -143.27                                   
REMARK 500    ARG E 105     -102.38     56.18                                   
REMARK 500    ASP E 123     -136.09     59.87                                   
REMARK 500    LEU E 216       10.07     53.12                                   
REMARK 500    MET E 353       96.40    -60.39                                   
REMARK 500    ASN E 384     -106.90     54.79                                   
REMARK 500    PRO E 397       86.64    -67.76                                   
REMARK 500    CYS E 467     -163.39   -127.75                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     119 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 441   SG                                                     
REMARK 620 2 HEM A 601   NA   91.9                                              
REMARK 620 3 HEM A 601   NB   90.2  89.7                                        
REMARK 620 4 HEM A 601   NC   89.3 178.8  90.3                                  
REMARK 620 5 HEM A 601   ND   90.5  89.1 178.7  90.9                            
REMARK 620 6 RIT A 602   N5  172.6  82.6  94.6  96.2  84.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 441   SG                                                     
REMARK 620 2 HEM B 601   NA   92.0                                              
REMARK 620 3 HEM B 601   NB   88.5  89.9                                        
REMARK 620 4 HEM B 601   NC   89.2 178.4  89.2                                  
REMARK 620 5 HEM B 601   ND   93.8  90.7 177.6  90.2                            
REMARK 620 6 RIT B 602   N5  175.7  83.7  91.0  95.0  86.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 441   SG                                                     
REMARK 620 2 HEM C 601   NA   94.7                                              
REMARK 620 3 HEM C 601   NB   83.2  90.0                                        
REMARK 620 4 HEM C 601   NC   85.7 179.5  90.1                                  
REMARK 620 5 HEM C 601   ND   97.2  89.8 179.6  90.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM D 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 441   SG                                                     
REMARK 620 2 HEM D 601   NA   92.4                                              
REMARK 620 3 HEM D 601   NB   86.8  90.0                                        
REMARK 620 4 HEM D 601   NC   86.3 178.7  89.8                                  
REMARK 620 5 HEM D 601   ND   91.3  90.6 178.0  89.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM E 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E 441   SG                                                     
REMARK 620 2 HEM E 601   NA   88.5                                              
REMARK 620 3 HEM E 601   NB   93.5  90.9                                        
REMARK 620 4 HEM E 601   NC   94.4 176.9  90.1                                  
REMARK 620 5 HEM E 601   ND   90.1  88.9 176.4  89.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM F 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F 441   SG                                                     
REMARK 620 2 HEM F 601   NA   85.9                                              
REMARK 620 3 HEM F 601   NB   80.2  90.6                                        
REMARK 620 4 HEM F 601   NC   95.5 178.4  90.4                                  
REMARK 620 5 HEM F 601   ND  100.5  89.1 179.2  89.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM G 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G 441   SG                                                     
REMARK 620 2 HEM G 601   NA   92.0                                              
REMARK 620 3 HEM G 601   NB   85.2  89.7                                        
REMARK 620 4 HEM G 601   NC   88.4 179.1  89.5                                  
REMARK 620 5 HEM G 601   ND   94.1  90.2 179.3  90.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM H 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS H 441   SG                                                     
REMARK 620 2 HEM H 601   NA   92.5                                              
REMARK 620 3 HEM H 601   NB   91.9  86.7                                        
REMARK 620 4 HEM H 601   NC   94.6 172.0  89.4                                  
REMARK 620 5 HEM H 601   ND   96.0  94.2 172.0  88.7                            
REMARK 620 6 RIT H 602   N5  173.1  94.4  89.0  78.6  83.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM I 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS I 441   SG                                                     
REMARK 620 2 HEM I 601   NA   92.8                                              
REMARK 620 3 HEM I 601   NB   86.3  90.3                                        
REMARK 620 4 HEM I 601   NC   87.3 179.6  90.1                                  
REMARK 620 5 HEM I 601   ND   93.4  89.3 179.5  90.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM J 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS J 441   SG                                                     
REMARK 620 2 HEM J 601   NA   93.4                                              
REMARK 620 3 HEM J 601   NB   91.8  89.4                                        
REMARK 620 4 HEM J 601   NC   84.2 177.5  90.6                                  
REMARK 620 5 HEM J 601   ND   85.7  89.9 177.4  90.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM K 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS K 441   SG                                                     
REMARK 620 2 HEM K 601   NA   90.3                                              
REMARK 620 3 HEM K 601   NB   86.0  90.4                                        
REMARK 620 4 HEM K 601   NC   89.5 179.2  90.3                                  
REMARK 620 5 HEM K 601   ND   93.3  89.5 179.2  89.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM L 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS L 441   SG                                                     
REMARK 620 2 HEM L 601   NA   80.3                                              
REMARK 620 3 HEM L 601   NB   86.5  89.7                                        
REMARK 620 4 HEM L 601   NC  101.1 178.5  90.0                                  
REMARK 620 5 HEM L 601   ND   94.0  89.6 179.0  90.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE INHIBITOR                                
REMARK 630 MOLECULE NAME: RITONAVIR                                             
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     RIT A   602                                                      
REMARK 630     RIT B   602                                                      
REMARK 630     RIT H   602                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    013 015 VAL 019                                          
REMARK 630 DETAILS: NULL                                                        
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue RIT A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue RIT B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM D 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM E 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM F 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM G 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM H 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue RIT H 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM I 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM J 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM K 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM L 601                 
DBREF  5VEU A   24   497  UNP    P20815   CP3A5_HUMAN     24    497             
DBREF  5VEU B   24   497  UNP    P20815   CP3A5_HUMAN     24    497             
DBREF  5VEU C   24   497  UNP    P20815   CP3A5_HUMAN     24    497             
DBREF  5VEU D   24   497  UNP    P20815   CP3A5_HUMAN     24    497             
DBREF  5VEU E   24   497  UNP    P20815   CP3A5_HUMAN     24    497             
DBREF  5VEU F   24   497  UNP    P20815   CP3A5_HUMAN     24    497             
DBREF  5VEU G   24   497  UNP    P20815   CP3A5_HUMAN     24    497             
DBREF  5VEU H   24   497  UNP    P20815   CP3A5_HUMAN     24    497             
DBREF  5VEU I   24   497  UNP    P20815   CP3A5_HUMAN     24    497             
DBREF  5VEU J   24   497  UNP    P20815   CP3A5_HUMAN     24    497             
DBREF  5VEU K   24   497  UNP    P20815   CP3A5_HUMAN     24    497             
DBREF  5VEU L   24   497  UNP    P20815   CP3A5_HUMAN     24    497             
SEQADV 5VEU MET A   22  UNP  P20815              INITIATING METHIONINE          
SEQADV 5VEU ALA A   23  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS A  498  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS A  499  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS A  500  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS A  501  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU MET B   22  UNP  P20815              INITIATING METHIONINE          
SEQADV 5VEU ALA B   23  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS B  498  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS B  499  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS B  500  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS B  501  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU MET C   22  UNP  P20815              INITIATING METHIONINE          
SEQADV 5VEU ALA C   23  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS C  498  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS C  499  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS C  500  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS C  501  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU MET D   22  UNP  P20815              INITIATING METHIONINE          
SEQADV 5VEU ALA D   23  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS D  498  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS D  499  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS D  500  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS D  501  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU MET E   22  UNP  P20815              INITIATING METHIONINE          
SEQADV 5VEU ALA E   23  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS E  498  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS E  499  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS E  500  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS E  501  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU MET F   22  UNP  P20815              INITIATING METHIONINE          
SEQADV 5VEU ALA F   23  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS F  498  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS F  499  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS F  500  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS F  501  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU MET G   22  UNP  P20815              INITIATING METHIONINE          
SEQADV 5VEU ALA G   23  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS G  498  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS G  499  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS G  500  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS G  501  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU MET H   22  UNP  P20815              INITIATING METHIONINE          
SEQADV 5VEU ALA H   23  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS H  498  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS H  499  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS H  500  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS H  501  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU MET I   22  UNP  P20815              INITIATING METHIONINE          
SEQADV 5VEU ALA I   23  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS I  498  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS I  499  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS I  500  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS I  501  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU MET J   22  UNP  P20815              INITIATING METHIONINE          
SEQADV 5VEU ALA J   23  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS J  498  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS J  499  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS J  500  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS J  501  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU MET K   22  UNP  P20815              INITIATING METHIONINE          
SEQADV 5VEU ALA K   23  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS K  498  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS K  499  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS K  500  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS K  501  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU MET L   22  UNP  P20815              INITIATING METHIONINE          
SEQADV 5VEU ALA L   23  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS L  498  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS L  499  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS L  500  UNP  P20815              EXPRESSION TAG                 
SEQADV 5VEU HIS L  501  UNP  P20815              EXPRESSION TAG                 
SEQRES   1 A  480  MET ALA LEU TYR GLY THR ARG THR HIS GLY LEU PHE LYS          
SEQRES   2 A  480  ARG LEU GLY ILE PRO GLY PRO THR PRO LEU PRO LEU LEU          
SEQRES   3 A  480  GLY ASN VAL LEU SER TYR ARG GLN GLY LEU TRP LYS PHE          
SEQRES   4 A  480  ASP THR GLU CYS TYR LYS LYS TYR GLY LYS MET TRP GLY          
SEQRES   5 A  480  THR TYR GLU GLY GLN LEU PRO VAL LEU ALA ILE THR ASP          
SEQRES   6 A  480  PRO ASP VAL ILE ARG THR VAL LEU VAL LYS GLU CYS TYR          
SEQRES   7 A  480  SER VAL PHE THR ASN ARG ARG SER LEU GLY PRO VAL GLY          
SEQRES   8 A  480  PHE MET LYS SER ALA ILE SER LEU ALA GLU ASP GLU GLU          
SEQRES   9 A  480  TRP LYS ARG ILE ARG SER LEU LEU SER PRO THR PHE THR          
SEQRES  10 A  480  SER GLY LYS LEU LYS GLU MET PHE PRO ILE ILE ALA GLN          
SEQRES  11 A  480  TYR GLY ASP VAL LEU VAL ARG ASN LEU ARG ARG GLU ALA          
SEQRES  12 A  480  GLU LYS GLY LYS PRO VAL THR LEU LYS ASP ILE PHE GLY          
SEQRES  13 A  480  ALA TYR SER MET ASP VAL ILE THR GLY THR SER PHE GLY          
SEQRES  14 A  480  VAL ASN ILE ASP SER LEU ASN ASN PRO GLN ASP PRO PHE          
SEQRES  15 A  480  VAL GLU SER THR LYS LYS PHE LEU LYS PHE GLY PHE LEU          
SEQRES  16 A  480  ASP PRO LEU PHE LEU SER ILE ILE LEU PHE PRO PHE LEU          
SEQRES  17 A  480  THR PRO VAL PHE GLU ALA LEU ASN VAL SER LEU PHE PRO          
SEQRES  18 A  480  LYS ASP THR ILE ASN PHE LEU SER LYS SER VAL ASN ARG          
SEQRES  19 A  480  MET LYS LYS SER ARG LEU ASN ASP LYS GLN LYS HIS ARG          
SEQRES  20 A  480  LEU ASP PHE LEU GLN LEU MET ILE ASP SER GLN ASN SER          
SEQRES  21 A  480  LYS GLU THR GLU SER HIS LYS ALA LEU SER ASP LEU GLU          
SEQRES  22 A  480  LEU ALA ALA GLN SER ILE ILE PHE ILE PHE ALA GLY TYR          
SEQRES  23 A  480  GLU THR THR SER SER VAL LEU SER PHE THR LEU TYR GLU          
SEQRES  24 A  480  LEU ALA THR HIS PRO ASP VAL GLN GLN LYS LEU GLN LYS          
SEQRES  25 A  480  GLU ILE ASP ALA VAL LEU PRO ASN LYS ALA PRO PRO THR          
SEQRES  26 A  480  TYR ASP ALA VAL VAL GLN MET GLU TYR LEU ASP MET VAL          
SEQRES  27 A  480  VAL ASN GLU THR LEU ARG LEU PHE PRO VAL ALA ILE ARG          
SEQRES  28 A  480  LEU GLU ARG THR CYS LYS LYS ASP VAL GLU ILE ASN GLY          
SEQRES  29 A  480  VAL PHE ILE PRO LYS GLY SER MET VAL VAL ILE PRO THR          
SEQRES  30 A  480  TYR ALA LEU HIS HIS ASP PRO LYS TYR TRP THR GLU PRO          
SEQRES  31 A  480  GLU GLU PHE ARG PRO GLU ARG PHE SER LYS LYS LYS ASP          
SEQRES  32 A  480  SER ILE ASP PRO TYR ILE TYR THR PRO PHE GLY THR GLY          
SEQRES  33 A  480  PRO ARG ASN CYS ILE GLY MET ARG PHE ALA LEU MET ASN          
SEQRES  34 A  480  MET LYS LEU ALA LEU ILE ARG VAL LEU GLN ASN PHE SER          
SEQRES  35 A  480  PHE LYS PRO CYS LYS GLU THR GLN ILE PRO LEU LYS LEU          
SEQRES  36 A  480  ASP THR GLN GLY LEU LEU GLN PRO GLU LYS PRO ILE VAL          
SEQRES  37 A  480  LEU LYS VAL ASP SER ARG ASP GLY HIS HIS HIS HIS              
SEQRES   1 B  480  MET ALA LEU TYR GLY THR ARG THR HIS GLY LEU PHE LYS          
SEQRES   2 B  480  ARG LEU GLY ILE PRO GLY PRO THR PRO LEU PRO LEU LEU          
SEQRES   3 B  480  GLY ASN VAL LEU SER TYR ARG GLN GLY LEU TRP LYS PHE          
SEQRES   4 B  480  ASP THR GLU CYS TYR LYS LYS TYR GLY LYS MET TRP GLY          
SEQRES   5 B  480  THR TYR GLU GLY GLN LEU PRO VAL LEU ALA ILE THR ASP          
SEQRES   6 B  480  PRO ASP VAL ILE ARG THR VAL LEU VAL LYS GLU CYS TYR          
SEQRES   7 B  480  SER VAL PHE THR ASN ARG ARG SER LEU GLY PRO VAL GLY          
SEQRES   8 B  480  PHE MET LYS SER ALA ILE SER LEU ALA GLU ASP GLU GLU          
SEQRES   9 B  480  TRP LYS ARG ILE ARG SER LEU LEU SER PRO THR PHE THR          
SEQRES  10 B  480  SER GLY LYS LEU LYS GLU MET PHE PRO ILE ILE ALA GLN          
SEQRES  11 B  480  TYR GLY ASP VAL LEU VAL ARG ASN LEU ARG ARG GLU ALA          
SEQRES  12 B  480  GLU LYS GLY LYS PRO VAL THR LEU LYS ASP ILE PHE GLY          
SEQRES  13 B  480  ALA TYR SER MET ASP VAL ILE THR GLY THR SER PHE GLY          
SEQRES  14 B  480  VAL ASN ILE ASP SER LEU ASN ASN PRO GLN ASP PRO PHE          
SEQRES  15 B  480  VAL GLU SER THR LYS LYS PHE LEU LYS PHE GLY PHE LEU          
SEQRES  16 B  480  ASP PRO LEU PHE LEU SER ILE ILE LEU PHE PRO PHE LEU          
SEQRES  17 B  480  THR PRO VAL PHE GLU ALA LEU ASN VAL SER LEU PHE PRO          
SEQRES  18 B  480  LYS ASP THR ILE ASN PHE LEU SER LYS SER VAL ASN ARG          
SEQRES  19 B  480  MET LYS LYS SER ARG LEU ASN ASP LYS GLN LYS HIS ARG          
SEQRES  20 B  480  LEU ASP PHE LEU GLN LEU MET ILE ASP SER GLN ASN SER          
SEQRES  21 B  480  LYS GLU THR GLU SER HIS LYS ALA LEU SER ASP LEU GLU          
SEQRES  22 B  480  LEU ALA ALA GLN SER ILE ILE PHE ILE PHE ALA GLY TYR          
SEQRES  23 B  480  GLU THR THR SER SER VAL LEU SER PHE THR LEU TYR GLU          
SEQRES  24 B  480  LEU ALA THR HIS PRO ASP VAL GLN GLN LYS LEU GLN LYS          
SEQRES  25 B  480  GLU ILE ASP ALA VAL LEU PRO ASN LYS ALA PRO PRO THR          
SEQRES  26 B  480  TYR ASP ALA VAL VAL GLN MET GLU TYR LEU ASP MET VAL          
SEQRES  27 B  480  VAL ASN GLU THR LEU ARG LEU PHE PRO VAL ALA ILE ARG          
SEQRES  28 B  480  LEU GLU ARG THR CYS LYS LYS ASP VAL GLU ILE ASN GLY          
SEQRES  29 B  480  VAL PHE ILE PRO LYS GLY SER MET VAL VAL ILE PRO THR          
SEQRES  30 B  480  TYR ALA LEU HIS HIS ASP PRO LYS TYR TRP THR GLU PRO          
SEQRES  31 B  480  GLU GLU PHE ARG PRO GLU ARG PHE SER LYS LYS LYS ASP          
SEQRES  32 B  480  SER ILE ASP PRO TYR ILE TYR THR PRO PHE GLY THR GLY          
SEQRES  33 B  480  PRO ARG ASN CYS ILE GLY MET ARG PHE ALA LEU MET ASN          
SEQRES  34 B  480  MET LYS LEU ALA LEU ILE ARG VAL LEU GLN ASN PHE SER          
SEQRES  35 B  480  PHE LYS PRO CYS LYS GLU THR GLN ILE PRO LEU LYS LEU          
SEQRES  36 B  480  ASP THR GLN GLY LEU LEU GLN PRO GLU LYS PRO ILE VAL          
SEQRES  37 B  480  LEU LYS VAL ASP SER ARG ASP GLY HIS HIS HIS HIS              
SEQRES   1 C  480  MET ALA LEU TYR GLY THR ARG THR HIS GLY LEU PHE LYS          
SEQRES   2 C  480  ARG LEU GLY ILE PRO GLY PRO THR PRO LEU PRO LEU LEU          
SEQRES   3 C  480  GLY ASN VAL LEU SER TYR ARG GLN GLY LEU TRP LYS PHE          
SEQRES   4 C  480  ASP THR GLU CYS TYR LYS LYS TYR GLY LYS MET TRP GLY          
SEQRES   5 C  480  THR TYR GLU GLY GLN LEU PRO VAL LEU ALA ILE THR ASP          
SEQRES   6 C  480  PRO ASP VAL ILE ARG THR VAL LEU VAL LYS GLU CYS TYR          
SEQRES   7 C  480  SER VAL PHE THR ASN ARG ARG SER LEU GLY PRO VAL GLY          
SEQRES   8 C  480  PHE MET LYS SER ALA ILE SER LEU ALA GLU ASP GLU GLU          
SEQRES   9 C  480  TRP LYS ARG ILE ARG SER LEU LEU SER PRO THR PHE THR          
SEQRES  10 C  480  SER GLY LYS LEU LYS GLU MET PHE PRO ILE ILE ALA GLN          
SEQRES  11 C  480  TYR GLY ASP VAL LEU VAL ARG ASN LEU ARG ARG GLU ALA          
SEQRES  12 C  480  GLU LYS GLY LYS PRO VAL THR LEU LYS ASP ILE PHE GLY          
SEQRES  13 C  480  ALA TYR SER MET ASP VAL ILE THR GLY THR SER PHE GLY          
SEQRES  14 C  480  VAL ASN ILE ASP SER LEU ASN ASN PRO GLN ASP PRO PHE          
SEQRES  15 C  480  VAL GLU SER THR LYS LYS PHE LEU LYS PHE GLY PHE LEU          
SEQRES  16 C  480  ASP PRO LEU PHE LEU SER ILE ILE LEU PHE PRO PHE LEU          
SEQRES  17 C  480  THR PRO VAL PHE GLU ALA LEU ASN VAL SER LEU PHE PRO          
SEQRES  18 C  480  LYS ASP THR ILE ASN PHE LEU SER LYS SER VAL ASN ARG          
SEQRES  19 C  480  MET LYS LYS SER ARG LEU ASN ASP LYS GLN LYS HIS ARG          
SEQRES  20 C  480  LEU ASP PHE LEU GLN LEU MET ILE ASP SER GLN ASN SER          
SEQRES  21 C  480  LYS GLU THR GLU SER HIS LYS ALA LEU SER ASP LEU GLU          
SEQRES  22 C  480  LEU ALA ALA GLN SER ILE ILE PHE ILE PHE ALA GLY TYR          
SEQRES  23 C  480  GLU THR THR SER SER VAL LEU SER PHE THR LEU TYR GLU          
SEQRES  24 C  480  LEU ALA THR HIS PRO ASP VAL GLN GLN LYS LEU GLN LYS          
SEQRES  25 C  480  GLU ILE ASP ALA VAL LEU PRO ASN LYS ALA PRO PRO THR          
SEQRES  26 C  480  TYR ASP ALA VAL VAL GLN MET GLU TYR LEU ASP MET VAL          
SEQRES  27 C  480  VAL ASN GLU THR LEU ARG LEU PHE PRO VAL ALA ILE ARG          
SEQRES  28 C  480  LEU GLU ARG THR CYS LYS LYS ASP VAL GLU ILE ASN GLY          
SEQRES  29 C  480  VAL PHE ILE PRO LYS GLY SER MET VAL VAL ILE PRO THR          
SEQRES  30 C  480  TYR ALA LEU HIS HIS ASP PRO LYS TYR TRP THR GLU PRO          
SEQRES  31 C  480  GLU GLU PHE ARG PRO GLU ARG PHE SER LYS LYS LYS ASP          
SEQRES  32 C  480  SER ILE ASP PRO TYR ILE TYR THR PRO PHE GLY THR GLY          
SEQRES  33 C  480  PRO ARG ASN CYS ILE GLY MET ARG PHE ALA LEU MET ASN          
SEQRES  34 C  480  MET LYS LEU ALA LEU ILE ARG VAL LEU GLN ASN PHE SER          
SEQRES  35 C  480  PHE LYS PRO CYS LYS GLU THR GLN ILE PRO LEU LYS LEU          
SEQRES  36 C  480  ASP THR GLN GLY LEU LEU GLN PRO GLU LYS PRO ILE VAL          
SEQRES  37 C  480  LEU LYS VAL ASP SER ARG ASP GLY HIS HIS HIS HIS              
SEQRES   1 D  480  MET ALA LEU TYR GLY THR ARG THR HIS GLY LEU PHE LYS          
SEQRES   2 D  480  ARG LEU GLY ILE PRO GLY PRO THR PRO LEU PRO LEU LEU          
SEQRES   3 D  480  GLY ASN VAL LEU SER TYR ARG GLN GLY LEU TRP LYS PHE          
SEQRES   4 D  480  ASP THR GLU CYS TYR LYS LYS TYR GLY LYS MET TRP GLY          
SEQRES   5 D  480  THR TYR GLU GLY GLN LEU PRO VAL LEU ALA ILE THR ASP          
SEQRES   6 D  480  PRO ASP VAL ILE ARG THR VAL LEU VAL LYS GLU CYS TYR          
SEQRES   7 D  480  SER VAL PHE THR ASN ARG ARG SER LEU GLY PRO VAL GLY          
SEQRES   8 D  480  PHE MET LYS SER ALA ILE SER LEU ALA GLU ASP GLU GLU          
SEQRES   9 D  480  TRP LYS ARG ILE ARG SER LEU LEU SER PRO THR PHE THR          
SEQRES  10 D  480  SER GLY LYS LEU LYS GLU MET PHE PRO ILE ILE ALA GLN          
SEQRES  11 D  480  TYR GLY ASP VAL LEU VAL ARG ASN LEU ARG ARG GLU ALA          
SEQRES  12 D  480  GLU LYS GLY LYS PRO VAL THR LEU LYS ASP ILE PHE GLY          
SEQRES  13 D  480  ALA TYR SER MET ASP VAL ILE THR GLY THR SER PHE GLY          
SEQRES  14 D  480  VAL ASN ILE ASP SER LEU ASN ASN PRO GLN ASP PRO PHE          
SEQRES  15 D  480  VAL GLU SER THR LYS LYS PHE LEU LYS PHE GLY PHE LEU          
SEQRES  16 D  480  ASP PRO LEU PHE LEU SER ILE ILE LEU PHE PRO PHE LEU          
SEQRES  17 D  480  THR PRO VAL PHE GLU ALA LEU ASN VAL SER LEU PHE PRO          
SEQRES  18 D  480  LYS ASP THR ILE ASN PHE LEU SER LYS SER VAL ASN ARG          
SEQRES  19 D  480  MET LYS LYS SER ARG LEU ASN ASP LYS GLN LYS HIS ARG          
SEQRES  20 D  480  LEU ASP PHE LEU GLN LEU MET ILE ASP SER GLN ASN SER          
SEQRES  21 D  480  LYS GLU THR GLU SER HIS LYS ALA LEU SER ASP LEU GLU          
SEQRES  22 D  480  LEU ALA ALA GLN SER ILE ILE PHE ILE PHE ALA GLY TYR          
SEQRES  23 D  480  GLU THR THR SER SER VAL LEU SER PHE THR LEU TYR GLU          
SEQRES  24 D  480  LEU ALA THR HIS PRO ASP VAL GLN GLN LYS LEU GLN LYS          
SEQRES  25 D  480  GLU ILE ASP ALA VAL LEU PRO ASN LYS ALA PRO PRO THR          
SEQRES  26 D  480  TYR ASP ALA VAL VAL GLN MET GLU TYR LEU ASP MET VAL          
SEQRES  27 D  480  VAL ASN GLU THR LEU ARG LEU PHE PRO VAL ALA ILE ARG          
SEQRES  28 D  480  LEU GLU ARG THR CYS LYS LYS ASP VAL GLU ILE ASN GLY          
SEQRES  29 D  480  VAL PHE ILE PRO LYS GLY SER MET VAL VAL ILE PRO THR          
SEQRES  30 D  480  TYR ALA LEU HIS HIS ASP PRO LYS TYR TRP THR GLU PRO          
SEQRES  31 D  480  GLU GLU PHE ARG PRO GLU ARG PHE SER LYS LYS LYS ASP          
SEQRES  32 D  480  SER ILE ASP PRO TYR ILE TYR THR PRO PHE GLY THR GLY          
SEQRES  33 D  480  PRO ARG ASN CYS ILE GLY MET ARG PHE ALA LEU MET ASN          
SEQRES  34 D  480  MET LYS LEU ALA LEU ILE ARG VAL LEU GLN ASN PHE SER          
SEQRES  35 D  480  PHE LYS PRO CYS LYS GLU THR GLN ILE PRO LEU LYS LEU          
SEQRES  36 D  480  ASP THR GLN GLY LEU LEU GLN PRO GLU LYS PRO ILE VAL          
SEQRES  37 D  480  LEU LYS VAL ASP SER ARG ASP GLY HIS HIS HIS HIS              
SEQRES   1 E  480  MET ALA LEU TYR GLY THR ARG THR HIS GLY LEU PHE LYS          
SEQRES   2 E  480  ARG LEU GLY ILE PRO GLY PRO THR PRO LEU PRO LEU LEU          
SEQRES   3 E  480  GLY ASN VAL LEU SER TYR ARG GLN GLY LEU TRP LYS PHE          
SEQRES   4 E  480  ASP THR GLU CYS TYR LYS LYS TYR GLY LYS MET TRP GLY          
SEQRES   5 E  480  THR TYR GLU GLY GLN LEU PRO VAL LEU ALA ILE THR ASP          
SEQRES   6 E  480  PRO ASP VAL ILE ARG THR VAL LEU VAL LYS GLU CYS TYR          
SEQRES   7 E  480  SER VAL PHE THR ASN ARG ARG SER LEU GLY PRO VAL GLY          
SEQRES   8 E  480  PHE MET LYS SER ALA ILE SER LEU ALA GLU ASP GLU GLU          
SEQRES   9 E  480  TRP LYS ARG ILE ARG SER LEU LEU SER PRO THR PHE THR          
SEQRES  10 E  480  SER GLY LYS LEU LYS GLU MET PHE PRO ILE ILE ALA GLN          
SEQRES  11 E  480  TYR GLY ASP VAL LEU VAL ARG ASN LEU ARG ARG GLU ALA          
SEQRES  12 E  480  GLU LYS GLY LYS PRO VAL THR LEU LYS ASP ILE PHE GLY          
SEQRES  13 E  480  ALA TYR SER MET ASP VAL ILE THR GLY THR SER PHE GLY          
SEQRES  14 E  480  VAL ASN ILE ASP SER LEU ASN ASN PRO GLN ASP PRO PHE          
SEQRES  15 E  480  VAL GLU SER THR LYS LYS PHE LEU LYS PHE GLY PHE LEU          
SEQRES  16 E  480  ASP PRO LEU PHE LEU SER ILE ILE LEU PHE PRO PHE LEU          
SEQRES  17 E  480  THR PRO VAL PHE GLU ALA LEU ASN VAL SER LEU PHE PRO          
SEQRES  18 E  480  LYS ASP THR ILE ASN PHE LEU SER LYS SER VAL ASN ARG          
SEQRES  19 E  480  MET LYS LYS SER ARG LEU ASN ASP LYS GLN LYS HIS ARG          
SEQRES  20 E  480  LEU ASP PHE LEU GLN LEU MET ILE ASP SER GLN ASN SER          
SEQRES  21 E  480  LYS GLU THR GLU SER HIS LYS ALA LEU SER ASP LEU GLU          
SEQRES  22 E  480  LEU ALA ALA GLN SER ILE ILE PHE ILE PHE ALA GLY TYR          
SEQRES  23 E  480  GLU THR THR SER SER VAL LEU SER PHE THR LEU TYR GLU          
SEQRES  24 E  480  LEU ALA THR HIS PRO ASP VAL GLN GLN LYS LEU GLN LYS          
SEQRES  25 E  480  GLU ILE ASP ALA VAL LEU PRO ASN LYS ALA PRO PRO THR          
SEQRES  26 E  480  TYR ASP ALA VAL VAL GLN MET GLU TYR LEU ASP MET VAL          
SEQRES  27 E  480  VAL ASN GLU THR LEU ARG LEU PHE PRO VAL ALA ILE ARG          
SEQRES  28 E  480  LEU GLU ARG THR CYS LYS LYS ASP VAL GLU ILE ASN GLY          
SEQRES  29 E  480  VAL PHE ILE PRO LYS GLY SER MET VAL VAL ILE PRO THR          
SEQRES  30 E  480  TYR ALA LEU HIS HIS ASP PRO LYS TYR TRP THR GLU PRO          
SEQRES  31 E  480  GLU GLU PHE ARG PRO GLU ARG PHE SER LYS LYS LYS ASP          
SEQRES  32 E  480  SER ILE ASP PRO TYR ILE TYR THR PRO PHE GLY THR GLY          
SEQRES  33 E  480  PRO ARG ASN CYS ILE GLY MET ARG PHE ALA LEU MET ASN          
SEQRES  34 E  480  MET LYS LEU ALA LEU ILE ARG VAL LEU GLN ASN PHE SER          
SEQRES  35 E  480  PHE LYS PRO CYS LYS GLU THR GLN ILE PRO LEU LYS LEU          
SEQRES  36 E  480  ASP THR GLN GLY LEU LEU GLN PRO GLU LYS PRO ILE VAL          
SEQRES  37 E  480  LEU LYS VAL ASP SER ARG ASP GLY HIS HIS HIS HIS              
SEQRES   1 F  480  MET ALA LEU TYR GLY THR ARG THR HIS GLY LEU PHE LYS          
SEQRES   2 F  480  ARG LEU GLY ILE PRO GLY PRO THR PRO LEU PRO LEU LEU          
SEQRES   3 F  480  GLY ASN VAL LEU SER TYR ARG GLN GLY LEU TRP LYS PHE          
SEQRES   4 F  480  ASP THR GLU CYS TYR LYS LYS TYR GLY LYS MET TRP GLY          
SEQRES   5 F  480  THR TYR GLU GLY GLN LEU PRO VAL LEU ALA ILE THR ASP          
SEQRES   6 F  480  PRO ASP VAL ILE ARG THR VAL LEU VAL LYS GLU CYS TYR          
SEQRES   7 F  480  SER VAL PHE THR ASN ARG ARG SER LEU GLY PRO VAL GLY          
SEQRES   8 F  480  PHE MET LYS SER ALA ILE SER LEU ALA GLU ASP GLU GLU          
SEQRES   9 F  480  TRP LYS ARG ILE ARG SER LEU LEU SER PRO THR PHE THR          
SEQRES  10 F  480  SER GLY LYS LEU LYS GLU MET PHE PRO ILE ILE ALA GLN          
SEQRES  11 F  480  TYR GLY ASP VAL LEU VAL ARG ASN LEU ARG ARG GLU ALA          
SEQRES  12 F  480  GLU LYS GLY LYS PRO VAL THR LEU LYS ASP ILE PHE GLY          
SEQRES  13 F  480  ALA TYR SER MET ASP VAL ILE THR GLY THR SER PHE GLY          
SEQRES  14 F  480  VAL ASN ILE ASP SER LEU ASN ASN PRO GLN ASP PRO PHE          
SEQRES  15 F  480  VAL GLU SER THR LYS LYS PHE LEU LYS PHE GLY PHE LEU          
SEQRES  16 F  480  ASP PRO LEU PHE LEU SER ILE ILE LEU PHE PRO PHE LEU          
SEQRES  17 F  480  THR PRO VAL PHE GLU ALA LEU ASN VAL SER LEU PHE PRO          
SEQRES  18 F  480  LYS ASP THR ILE ASN PHE LEU SER LYS SER VAL ASN ARG          
SEQRES  19 F  480  MET LYS LYS SER ARG LEU ASN ASP LYS GLN LYS HIS ARG          
SEQRES  20 F  480  LEU ASP PHE LEU GLN LEU MET ILE ASP SER GLN ASN SER          
SEQRES  21 F  480  LYS GLU THR GLU SER HIS LYS ALA LEU SER ASP LEU GLU          
SEQRES  22 F  480  LEU ALA ALA GLN SER ILE ILE PHE ILE PHE ALA GLY TYR          
SEQRES  23 F  480  GLU THR THR SER SER VAL LEU SER PHE THR LEU TYR GLU          
SEQRES  24 F  480  LEU ALA THR HIS PRO ASP VAL GLN GLN LYS LEU GLN LYS          
SEQRES  25 F  480  GLU ILE ASP ALA VAL LEU PRO ASN LYS ALA PRO PRO THR          
SEQRES  26 F  480  TYR ASP ALA VAL VAL GLN MET GLU TYR LEU ASP MET VAL          
SEQRES  27 F  480  VAL ASN GLU THR LEU ARG LEU PHE PRO VAL ALA ILE ARG          
SEQRES  28 F  480  LEU GLU ARG THR CYS LYS LYS ASP VAL GLU ILE ASN GLY          
SEQRES  29 F  480  VAL PHE ILE PRO LYS GLY SER MET VAL VAL ILE PRO THR          
SEQRES  30 F  480  TYR ALA LEU HIS HIS ASP PRO LYS TYR TRP THR GLU PRO          
SEQRES  31 F  480  GLU GLU PHE ARG PRO GLU ARG PHE SER LYS LYS LYS ASP          
SEQRES  32 F  480  SER ILE ASP PRO TYR ILE TYR THR PRO PHE GLY THR GLY          
SEQRES  33 F  480  PRO ARG ASN CYS ILE GLY MET ARG PHE ALA LEU MET ASN          
SEQRES  34 F  480  MET LYS LEU ALA LEU ILE ARG VAL LEU GLN ASN PHE SER          
SEQRES  35 F  480  PHE LYS PRO CYS LYS GLU THR GLN ILE PRO LEU LYS LEU          
SEQRES  36 F  480  ASP THR GLN GLY LEU LEU GLN PRO GLU LYS PRO ILE VAL          
SEQRES  37 F  480  LEU LYS VAL ASP SER ARG ASP GLY HIS HIS HIS HIS              
SEQRES   1 G  480  MET ALA LEU TYR GLY THR ARG THR HIS GLY LEU PHE LYS          
SEQRES   2 G  480  ARG LEU GLY ILE PRO GLY PRO THR PRO LEU PRO LEU LEU          
SEQRES   3 G  480  GLY ASN VAL LEU SER TYR ARG GLN GLY LEU TRP LYS PHE          
SEQRES   4 G  480  ASP THR GLU CYS TYR LYS LYS TYR GLY LYS MET TRP GLY          
SEQRES   5 G  480  THR TYR GLU GLY GLN LEU PRO VAL LEU ALA ILE THR ASP          
SEQRES   6 G  480  PRO ASP VAL ILE ARG THR VAL LEU VAL LYS GLU CYS TYR          
SEQRES   7 G  480  SER VAL PHE THR ASN ARG ARG SER LEU GLY PRO VAL GLY          
SEQRES   8 G  480  PHE MET LYS SER ALA ILE SER LEU ALA GLU ASP GLU GLU          
SEQRES   9 G  480  TRP LYS ARG ILE ARG SER LEU LEU SER PRO THR PHE THR          
SEQRES  10 G  480  SER GLY LYS LEU LYS GLU MET PHE PRO ILE ILE ALA GLN          
SEQRES  11 G  480  TYR GLY ASP VAL LEU VAL ARG ASN LEU ARG ARG GLU ALA          
SEQRES  12 G  480  GLU LYS GLY LYS PRO VAL THR LEU LYS ASP ILE PHE GLY          
SEQRES  13 G  480  ALA TYR SER MET ASP VAL ILE THR GLY THR SER PHE GLY          
SEQRES  14 G  480  VAL ASN ILE ASP SER LEU ASN ASN PRO GLN ASP PRO PHE          
SEQRES  15 G  480  VAL GLU SER THR LYS LYS PHE LEU LYS PHE GLY PHE LEU          
SEQRES  16 G  480  ASP PRO LEU PHE LEU SER ILE ILE LEU PHE PRO PHE LEU          
SEQRES  17 G  480  THR PRO VAL PHE GLU ALA LEU ASN VAL SER LEU PHE PRO          
SEQRES  18 G  480  LYS ASP THR ILE ASN PHE LEU SER LYS SER VAL ASN ARG          
SEQRES  19 G  480  MET LYS LYS SER ARG LEU ASN ASP LYS GLN LYS HIS ARG          
SEQRES  20 G  480  LEU ASP PHE LEU GLN LEU MET ILE ASP SER GLN ASN SER          
SEQRES  21 G  480  LYS GLU THR GLU SER HIS LYS ALA LEU SER ASP LEU GLU          
SEQRES  22 G  480  LEU ALA ALA GLN SER ILE ILE PHE ILE PHE ALA GLY TYR          
SEQRES  23 G  480  GLU THR THR SER SER VAL LEU SER PHE THR LEU TYR GLU          
SEQRES  24 G  480  LEU ALA THR HIS PRO ASP VAL GLN GLN LYS LEU GLN LYS          
SEQRES  25 G  480  GLU ILE ASP ALA VAL LEU PRO ASN LYS ALA PRO PRO THR          
SEQRES  26 G  480  TYR ASP ALA VAL VAL GLN MET GLU TYR LEU ASP MET VAL          
SEQRES  27 G  480  VAL ASN GLU THR LEU ARG LEU PHE PRO VAL ALA ILE ARG          
SEQRES  28 G  480  LEU GLU ARG THR CYS LYS LYS ASP VAL GLU ILE ASN GLY          
SEQRES  29 G  480  VAL PHE ILE PRO LYS GLY SER MET VAL VAL ILE PRO THR          
SEQRES  30 G  480  TYR ALA LEU HIS HIS ASP PRO LYS TYR TRP THR GLU PRO          
SEQRES  31 G  480  GLU GLU PHE ARG PRO GLU ARG PHE SER LYS LYS LYS ASP          
SEQRES  32 G  480  SER ILE ASP PRO TYR ILE TYR THR PRO PHE GLY THR GLY          
SEQRES  33 G  480  PRO ARG ASN CYS ILE GLY MET ARG PHE ALA LEU MET ASN          
SEQRES  34 G  480  MET LYS LEU ALA LEU ILE ARG VAL LEU GLN ASN PHE SER          
SEQRES  35 G  480  PHE LYS PRO CYS LYS GLU THR GLN ILE PRO LEU LYS LEU          
SEQRES  36 G  480  ASP THR GLN GLY LEU LEU GLN PRO GLU LYS PRO ILE VAL          
SEQRES  37 G  480  LEU LYS VAL ASP SER ARG ASP GLY HIS HIS HIS HIS              
SEQRES   1 H  480  MET ALA LEU TYR GLY THR ARG THR HIS GLY LEU PHE LYS          
SEQRES   2 H  480  ARG LEU GLY ILE PRO GLY PRO THR PRO LEU PRO LEU LEU          
SEQRES   3 H  480  GLY ASN VAL LEU SER TYR ARG GLN GLY LEU TRP LYS PHE          
SEQRES   4 H  480  ASP THR GLU CYS TYR LYS LYS TYR GLY LYS MET TRP GLY          
SEQRES   5 H  480  THR TYR GLU GLY GLN LEU PRO VAL LEU ALA ILE THR ASP          
SEQRES   6 H  480  PRO ASP VAL ILE ARG THR VAL LEU VAL LYS GLU CYS TYR          
SEQRES   7 H  480  SER VAL PHE THR ASN ARG ARG SER LEU GLY PRO VAL GLY          
SEQRES   8 H  480  PHE MET LYS SER ALA ILE SER LEU ALA GLU ASP GLU GLU          
SEQRES   9 H  480  TRP LYS ARG ILE ARG SER LEU LEU SER PRO THR PHE THR          
SEQRES  10 H  480  SER GLY LYS LEU LYS GLU MET PHE PRO ILE ILE ALA GLN          
SEQRES  11 H  480  TYR GLY ASP VAL LEU VAL ARG ASN LEU ARG ARG GLU ALA          
SEQRES  12 H  480  GLU LYS GLY LYS PRO VAL THR LEU LYS ASP ILE PHE GLY          
SEQRES  13 H  480  ALA TYR SER MET ASP VAL ILE THR GLY THR SER PHE GLY          
SEQRES  14 H  480  VAL ASN ILE ASP SER LEU ASN ASN PRO GLN ASP PRO PHE          
SEQRES  15 H  480  VAL GLU SER THR LYS LYS PHE LEU LYS PHE GLY PHE LEU          
SEQRES  16 H  480  ASP PRO LEU PHE LEU SER ILE ILE LEU PHE PRO PHE LEU          
SEQRES  17 H  480  THR PRO VAL PHE GLU ALA LEU ASN VAL SER LEU PHE PRO          
SEQRES  18 H  480  LYS ASP THR ILE ASN PHE LEU SER LYS SER VAL ASN ARG          
SEQRES  19 H  480  MET LYS LYS SER ARG LEU ASN ASP LYS GLN LYS HIS ARG          
SEQRES  20 H  480  LEU ASP PHE LEU GLN LEU MET ILE ASP SER GLN ASN SER          
SEQRES  21 H  480  LYS GLU THR GLU SER HIS LYS ALA LEU SER ASP LEU GLU          
SEQRES  22 H  480  LEU ALA ALA GLN SER ILE ILE PHE ILE PHE ALA GLY TYR          
SEQRES  23 H  480  GLU THR THR SER SER VAL LEU SER PHE THR LEU TYR GLU          
SEQRES  24 H  480  LEU ALA THR HIS PRO ASP VAL GLN GLN LYS LEU GLN LYS          
SEQRES  25 H  480  GLU ILE ASP ALA VAL LEU PRO ASN LYS ALA PRO PRO THR          
SEQRES  26 H  480  TYR ASP ALA VAL VAL GLN MET GLU TYR LEU ASP MET VAL          
SEQRES  27 H  480  VAL ASN GLU THR LEU ARG LEU PHE PRO VAL ALA ILE ARG          
SEQRES  28 H  480  LEU GLU ARG THR CYS LYS LYS ASP VAL GLU ILE ASN GLY          
SEQRES  29 H  480  VAL PHE ILE PRO LYS GLY SER MET VAL VAL ILE PRO THR          
SEQRES  30 H  480  TYR ALA LEU HIS HIS ASP PRO LYS TYR TRP THR GLU PRO          
SEQRES  31 H  480  GLU GLU PHE ARG PRO GLU ARG PHE SER LYS LYS LYS ASP          
SEQRES  32 H  480  SER ILE ASP PRO TYR ILE TYR THR PRO PHE GLY THR GLY          
SEQRES  33 H  480  PRO ARG ASN CYS ILE GLY MET ARG PHE ALA LEU MET ASN          
SEQRES  34 H  480  MET LYS LEU ALA LEU ILE ARG VAL LEU GLN ASN PHE SER          
SEQRES  35 H  480  PHE LYS PRO CYS LYS GLU THR GLN ILE PRO LEU LYS LEU          
SEQRES  36 H  480  ASP THR GLN GLY LEU LEU GLN PRO GLU LYS PRO ILE VAL          
SEQRES  37 H  480  LEU LYS VAL ASP SER ARG ASP GLY HIS HIS HIS HIS              
SEQRES   1 I  480  MET ALA LEU TYR GLY THR ARG THR HIS GLY LEU PHE LYS          
SEQRES   2 I  480  ARG LEU GLY ILE PRO GLY PRO THR PRO LEU PRO LEU LEU          
SEQRES   3 I  480  GLY ASN VAL LEU SER TYR ARG GLN GLY LEU TRP LYS PHE          
SEQRES   4 I  480  ASP THR GLU CYS TYR LYS LYS TYR GLY LYS MET TRP GLY          
SEQRES   5 I  480  THR TYR GLU GLY GLN LEU PRO VAL LEU ALA ILE THR ASP          
SEQRES   6 I  480  PRO ASP VAL ILE ARG THR VAL LEU VAL LYS GLU CYS TYR          
SEQRES   7 I  480  SER VAL PHE THR ASN ARG ARG SER LEU GLY PRO VAL GLY          
SEQRES   8 I  480  PHE MET LYS SER ALA ILE SER LEU ALA GLU ASP GLU GLU          
SEQRES   9 I  480  TRP LYS ARG ILE ARG SER LEU LEU SER PRO THR PHE THR          
SEQRES  10 I  480  SER GLY LYS LEU LYS GLU MET PHE PRO ILE ILE ALA GLN          
SEQRES  11 I  480  TYR GLY ASP VAL LEU VAL ARG ASN LEU ARG ARG GLU ALA          
SEQRES  12 I  480  GLU LYS GLY LYS PRO VAL THR LEU LYS ASP ILE PHE GLY          
SEQRES  13 I  480  ALA TYR SER MET ASP VAL ILE THR GLY THR SER PHE GLY          
SEQRES  14 I  480  VAL ASN ILE ASP SER LEU ASN ASN PRO GLN ASP PRO PHE          
SEQRES  15 I  480  VAL GLU SER THR LYS LYS PHE LEU LYS PHE GLY PHE LEU          
SEQRES  16 I  480  ASP PRO LEU PHE LEU SER ILE ILE LEU PHE PRO PHE LEU          
SEQRES  17 I  480  THR PRO VAL PHE GLU ALA LEU ASN VAL SER LEU PHE PRO          
SEQRES  18 I  480  LYS ASP THR ILE ASN PHE LEU SER LYS SER VAL ASN ARG          
SEQRES  19 I  480  MET LYS LYS SER ARG LEU ASN ASP LYS GLN LYS HIS ARG          
SEQRES  20 I  480  LEU ASP PHE LEU GLN LEU MET ILE ASP SER GLN ASN SER          
SEQRES  21 I  480  LYS GLU THR GLU SER HIS LYS ALA LEU SER ASP LEU GLU          
SEQRES  22 I  480  LEU ALA ALA GLN SER ILE ILE PHE ILE PHE ALA GLY TYR          
SEQRES  23 I  480  GLU THR THR SER SER VAL LEU SER PHE THR LEU TYR GLU          
SEQRES  24 I  480  LEU ALA THR HIS PRO ASP VAL GLN GLN LYS LEU GLN LYS          
SEQRES  25 I  480  GLU ILE ASP ALA VAL LEU PRO ASN LYS ALA PRO PRO THR          
SEQRES  26 I  480  TYR ASP ALA VAL VAL GLN MET GLU TYR LEU ASP MET VAL          
SEQRES  27 I  480  VAL ASN GLU THR LEU ARG LEU PHE PRO VAL ALA ILE ARG          
SEQRES  28 I  480  LEU GLU ARG THR CYS LYS LYS ASP VAL GLU ILE ASN GLY          
SEQRES  29 I  480  VAL PHE ILE PRO LYS GLY SER MET VAL VAL ILE PRO THR          
SEQRES  30 I  480  TYR ALA LEU HIS HIS ASP PRO LYS TYR TRP THR GLU PRO          
SEQRES  31 I  480  GLU GLU PHE ARG PRO GLU ARG PHE SER LYS LYS LYS ASP          
SEQRES  32 I  480  SER ILE ASP PRO TYR ILE TYR THR PRO PHE GLY THR GLY          
SEQRES  33 I  480  PRO ARG ASN CYS ILE GLY MET ARG PHE ALA LEU MET ASN          
SEQRES  34 I  480  MET LYS LEU ALA LEU ILE ARG VAL LEU GLN ASN PHE SER          
SEQRES  35 I  480  PHE LYS PRO CYS LYS GLU THR GLN ILE PRO LEU LYS LEU          
SEQRES  36 I  480  ASP THR GLN GLY LEU LEU GLN PRO GLU LYS PRO ILE VAL          
SEQRES  37 I  480  LEU LYS VAL ASP SER ARG ASP GLY HIS HIS HIS HIS              
SEQRES   1 J  480  MET ALA LEU TYR GLY THR ARG THR HIS GLY LEU PHE LYS          
SEQRES   2 J  480  ARG LEU GLY ILE PRO GLY PRO THR PRO LEU PRO LEU LEU          
SEQRES   3 J  480  GLY ASN VAL LEU SER TYR ARG GLN GLY LEU TRP LYS PHE          
SEQRES   4 J  480  ASP THR GLU CYS TYR LYS LYS TYR GLY LYS MET TRP GLY          
SEQRES   5 J  480  THR TYR GLU GLY GLN LEU PRO VAL LEU ALA ILE THR ASP          
SEQRES   6 J  480  PRO ASP VAL ILE ARG THR VAL LEU VAL LYS GLU CYS TYR          
SEQRES   7 J  480  SER VAL PHE THR ASN ARG ARG SER LEU GLY PRO VAL GLY          
SEQRES   8 J  480  PHE MET LYS SER ALA ILE SER LEU ALA GLU ASP GLU GLU          
SEQRES   9 J  480  TRP LYS ARG ILE ARG SER LEU LEU SER PRO THR PHE THR          
SEQRES  10 J  480  SER GLY LYS LEU LYS GLU MET PHE PRO ILE ILE ALA GLN          
SEQRES  11 J  480  TYR GLY ASP VAL LEU VAL ARG ASN LEU ARG ARG GLU ALA          
SEQRES  12 J  480  GLU LYS GLY LYS PRO VAL THR LEU LYS ASP ILE PHE GLY          
SEQRES  13 J  480  ALA TYR SER MET ASP VAL ILE THR GLY THR SER PHE GLY          
SEQRES  14 J  480  VAL ASN ILE ASP SER LEU ASN ASN PRO GLN ASP PRO PHE          
SEQRES  15 J  480  VAL GLU SER THR LYS LYS PHE LEU LYS PHE GLY PHE LEU          
SEQRES  16 J  480  ASP PRO LEU PHE LEU SER ILE ILE LEU PHE PRO PHE LEU          
SEQRES  17 J  480  THR PRO VAL PHE GLU ALA LEU ASN VAL SER LEU PHE PRO          
SEQRES  18 J  480  LYS ASP THR ILE ASN PHE LEU SER LYS SER VAL ASN ARG          
SEQRES  19 J  480  MET LYS LYS SER ARG LEU ASN ASP LYS GLN LYS HIS ARG          
SEQRES  20 J  480  LEU ASP PHE LEU GLN LEU MET ILE ASP SER GLN ASN SER          
SEQRES  21 J  480  LYS GLU THR GLU SER HIS LYS ALA LEU SER ASP LEU GLU          
SEQRES  22 J  480  LEU ALA ALA GLN SER ILE ILE PHE ILE PHE ALA GLY TYR          
SEQRES  23 J  480  GLU THR THR SER SER VAL LEU SER PHE THR LEU TYR GLU          
SEQRES  24 J  480  LEU ALA THR HIS PRO ASP VAL GLN GLN LYS LEU GLN LYS          
SEQRES  25 J  480  GLU ILE ASP ALA VAL LEU PRO ASN LYS ALA PRO PRO THR          
SEQRES  26 J  480  TYR ASP ALA VAL VAL GLN MET GLU TYR LEU ASP MET VAL          
SEQRES  27 J  480  VAL ASN GLU THR LEU ARG LEU PHE PRO VAL ALA ILE ARG          
SEQRES  28 J  480  LEU GLU ARG THR CYS LYS LYS ASP VAL GLU ILE ASN GLY          
SEQRES  29 J  480  VAL PHE ILE PRO LYS GLY SER MET VAL VAL ILE PRO THR          
SEQRES  30 J  480  TYR ALA LEU HIS HIS ASP PRO LYS TYR TRP THR GLU PRO          
SEQRES  31 J  480  GLU GLU PHE ARG PRO GLU ARG PHE SER LYS LYS LYS ASP          
SEQRES  32 J  480  SER ILE ASP PRO TYR ILE TYR THR PRO PHE GLY THR GLY          
SEQRES  33 J  480  PRO ARG ASN CYS ILE GLY MET ARG PHE ALA LEU MET ASN          
SEQRES  34 J  480  MET LYS LEU ALA LEU ILE ARG VAL LEU GLN ASN PHE SER          
SEQRES  35 J  480  PHE LYS PRO CYS LYS GLU THR GLN ILE PRO LEU LYS LEU          
SEQRES  36 J  480  ASP THR GLN GLY LEU LEU GLN PRO GLU LYS PRO ILE VAL          
SEQRES  37 J  480  LEU LYS VAL ASP SER ARG ASP GLY HIS HIS HIS HIS              
SEQRES   1 K  480  MET ALA LEU TYR GLY THR ARG THR HIS GLY LEU PHE LYS          
SEQRES   2 K  480  ARG LEU GLY ILE PRO GLY PRO THR PRO LEU PRO LEU LEU          
SEQRES   3 K  480  GLY ASN VAL LEU SER TYR ARG GLN GLY LEU TRP LYS PHE          
SEQRES   4 K  480  ASP THR GLU CYS TYR LYS LYS TYR GLY LYS MET TRP GLY          
SEQRES   5 K  480  THR TYR GLU GLY GLN LEU PRO VAL LEU ALA ILE THR ASP          
SEQRES   6 K  480  PRO ASP VAL ILE ARG THR VAL LEU VAL LYS GLU CYS TYR          
SEQRES   7 K  480  SER VAL PHE THR ASN ARG ARG SER LEU GLY PRO VAL GLY          
SEQRES   8 K  480  PHE MET LYS SER ALA ILE SER LEU ALA GLU ASP GLU GLU          
SEQRES   9 K  480  TRP LYS ARG ILE ARG SER LEU LEU SER PRO THR PHE THR          
SEQRES  10 K  480  SER GLY LYS LEU LYS GLU MET PHE PRO ILE ILE ALA GLN          
SEQRES  11 K  480  TYR GLY ASP VAL LEU VAL ARG ASN LEU ARG ARG GLU ALA          
SEQRES  12 K  480  GLU LYS GLY LYS PRO VAL THR LEU LYS ASP ILE PHE GLY          
SEQRES  13 K  480  ALA TYR SER MET ASP VAL ILE THR GLY THR SER PHE GLY          
SEQRES  14 K  480  VAL ASN ILE ASP SER LEU ASN ASN PRO GLN ASP PRO PHE          
SEQRES  15 K  480  VAL GLU SER THR LYS LYS PHE LEU LYS PHE GLY PHE LEU          
SEQRES  16 K  480  ASP PRO LEU PHE LEU SER ILE ILE LEU PHE PRO PHE LEU          
SEQRES  17 K  480  THR PRO VAL PHE GLU ALA LEU ASN VAL SER LEU PHE PRO          
SEQRES  18 K  480  LYS ASP THR ILE ASN PHE LEU SER LYS SER VAL ASN ARG          
SEQRES  19 K  480  MET LYS LYS SER ARG LEU ASN ASP LYS GLN LYS HIS ARG          
SEQRES  20 K  480  LEU ASP PHE LEU GLN LEU MET ILE ASP SER GLN ASN SER          
SEQRES  21 K  480  LYS GLU THR GLU SER HIS LYS ALA LEU SER ASP LEU GLU          
SEQRES  22 K  480  LEU ALA ALA GLN SER ILE ILE PHE ILE PHE ALA GLY TYR          
SEQRES  23 K  480  GLU THR THR SER SER VAL LEU SER PHE THR LEU TYR GLU          
SEQRES  24 K  480  LEU ALA THR HIS PRO ASP VAL GLN GLN LYS LEU GLN LYS          
SEQRES  25 K  480  GLU ILE ASP ALA VAL LEU PRO ASN LYS ALA PRO PRO THR          
SEQRES  26 K  480  TYR ASP ALA VAL VAL GLN MET GLU TYR LEU ASP MET VAL          
SEQRES  27 K  480  VAL ASN GLU THR LEU ARG LEU PHE PRO VAL ALA ILE ARG          
SEQRES  28 K  480  LEU GLU ARG THR CYS LYS LYS ASP VAL GLU ILE ASN GLY          
SEQRES  29 K  480  VAL PHE ILE PRO LYS GLY SER MET VAL VAL ILE PRO THR          
SEQRES  30 K  480  TYR ALA LEU HIS HIS ASP PRO LYS TYR TRP THR GLU PRO          
SEQRES  31 K  480  GLU GLU PHE ARG PRO GLU ARG PHE SER LYS LYS LYS ASP          
SEQRES  32 K  480  SER ILE ASP PRO TYR ILE TYR THR PRO PHE GLY THR GLY          
SEQRES  33 K  480  PRO ARG ASN CYS ILE GLY MET ARG PHE ALA LEU MET ASN          
SEQRES  34 K  480  MET LYS LEU ALA LEU ILE ARG VAL LEU GLN ASN PHE SER          
SEQRES  35 K  480  PHE LYS PRO CYS LYS GLU THR GLN ILE PRO LEU LYS LEU          
SEQRES  36 K  480  ASP THR GLN GLY LEU LEU GLN PRO GLU LYS PRO ILE VAL          
SEQRES  37 K  480  LEU LYS VAL ASP SER ARG ASP GLY HIS HIS HIS HIS              
SEQRES   1 L  480  MET ALA LEU TYR GLY THR ARG THR HIS GLY LEU PHE LYS          
SEQRES   2 L  480  ARG LEU GLY ILE PRO GLY PRO THR PRO LEU PRO LEU LEU          
SEQRES   3 L  480  GLY ASN VAL LEU SER TYR ARG GLN GLY LEU TRP LYS PHE          
SEQRES   4 L  480  ASP THR GLU CYS TYR LYS LYS TYR GLY LYS MET TRP GLY          
SEQRES   5 L  480  THR TYR GLU GLY GLN LEU PRO VAL LEU ALA ILE THR ASP          
SEQRES   6 L  480  PRO ASP VAL ILE ARG THR VAL LEU VAL LYS GLU CYS TYR          
SEQRES   7 L  480  SER VAL PHE THR ASN ARG ARG SER LEU GLY PRO VAL GLY          
SEQRES   8 L  480  PHE MET LYS SER ALA ILE SER LEU ALA GLU ASP GLU GLU          
SEQRES   9 L  480  TRP LYS ARG ILE ARG SER LEU LEU SER PRO THR PHE THR          
SEQRES  10 L  480  SER GLY LYS LEU LYS GLU MET PHE PRO ILE ILE ALA GLN          
SEQRES  11 L  480  TYR GLY ASP VAL LEU VAL ARG ASN LEU ARG ARG GLU ALA          
SEQRES  12 L  480  GLU LYS GLY LYS PRO VAL THR LEU LYS ASP ILE PHE GLY          
SEQRES  13 L  480  ALA TYR SER MET ASP VAL ILE THR GLY THR SER PHE GLY          
SEQRES  14 L  480  VAL ASN ILE ASP SER LEU ASN ASN PRO GLN ASP PRO PHE          
SEQRES  15 L  480  VAL GLU SER THR LYS LYS PHE LEU LYS PHE GLY PHE LEU          
SEQRES  16 L  480  ASP PRO LEU PHE LEU SER ILE ILE LEU PHE PRO PHE LEU          
SEQRES  17 L  480  THR PRO VAL PHE GLU ALA LEU ASN VAL SER LEU PHE PRO          
SEQRES  18 L  480  LYS ASP THR ILE ASN PHE LEU SER LYS SER VAL ASN ARG          
SEQRES  19 L  480  MET LYS LYS SER ARG LEU ASN ASP LYS GLN LYS HIS ARG          
SEQRES  20 L  480  LEU ASP PHE LEU GLN LEU MET ILE ASP SER GLN ASN SER          
SEQRES  21 L  480  LYS GLU THR GLU SER HIS LYS ALA LEU SER ASP LEU GLU          
SEQRES  22 L  480  LEU ALA ALA GLN SER ILE ILE PHE ILE PHE ALA GLY TYR          
SEQRES  23 L  480  GLU THR THR SER SER VAL LEU SER PHE THR LEU TYR GLU          
SEQRES  24 L  480  LEU ALA THR HIS PRO ASP VAL GLN GLN LYS LEU GLN LYS          
SEQRES  25 L  480  GLU ILE ASP ALA VAL LEU PRO ASN LYS ALA PRO PRO THR          
SEQRES  26 L  480  TYR ASP ALA VAL VAL GLN MET GLU TYR LEU ASP MET VAL          
SEQRES  27 L  480  VAL ASN GLU THR LEU ARG LEU PHE PRO VAL ALA ILE ARG          
SEQRES  28 L  480  LEU GLU ARG THR CYS LYS LYS ASP VAL GLU ILE ASN GLY          
SEQRES  29 L  480  VAL PHE ILE PRO LYS GLY SER MET VAL VAL ILE PRO THR          
SEQRES  30 L  480  TYR ALA LEU HIS HIS ASP PRO LYS TYR TRP THR GLU PRO          
SEQRES  31 L  480  GLU GLU PHE ARG PRO GLU ARG PHE SER LYS LYS LYS ASP          
SEQRES  32 L  480  SER ILE ASP PRO TYR ILE TYR THR PRO PHE GLY THR GLY          
SEQRES  33 L  480  PRO ARG ASN CYS ILE GLY MET ARG PHE ALA LEU MET ASN          
SEQRES  34 L  480  MET LYS LEU ALA LEU ILE ARG VAL LEU GLN ASN PHE SER          
SEQRES  35 L  480  PHE LYS PRO CYS LYS GLU THR GLN ILE PRO LEU LYS LEU          
SEQRES  36 L  480  ASP THR GLN GLY LEU LEU GLN PRO GLU LYS PRO ILE VAL          
SEQRES  37 L  480  LEU LYS VAL ASP SER ARG ASP GLY HIS HIS HIS HIS              
HET    HEM  A 601      43                                                       
HET    RIT  A 602      50                                                       
HET    HEM  B 601      43                                                       
HET    RIT  B 602      50                                                       
HET    HEM  C 601      43                                                       
HET    HEM  D 601      43                                                       
HET    HEM  E 601      43                                                       
HET    HEM  F 601      43                                                       
HET    HEM  G 601      43                                                       
HET    HEM  H 601      43                                                       
HET    RIT  H 602      50                                                       
HET    HEM  I 601      43                                                       
HET    HEM  J 601      43                                                       
HET    HEM  K 601      43                                                       
HET    HEM  L 601      43                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     RIT RITONAVIR                                                        
HETSYN     HEM HEME                                                             
HETSYN     RIT A-84538                                                          
FORMUL  13  HEM    12(C34 H32 FE N4 O4)                                         
FORMUL  14  RIT    3(C37 H48 N6 O5 S2)                                          
HELIX    1 AA1 GLY A   31  LEU A   36  1                                   6    
HELIX    2 AA2 ASN A   49  GLN A   55  5                                   7    
HELIX    3 AA3 GLY A   56  TYR A   68  1                                  13    
HELIX    4 AA4 ASP A   86  VAL A   95  1                                  10    
HELIX    5 AA5 VAL A  111  ALA A  117  5                                   7    
HELIX    6 AA6 GLU A  122  SER A  134  1                                  13    
HELIX    7 AA7 PRO A  135  PHE A  137  5                                   3    
HELIX    8 AA8 THR A  138  GLY A  167  1                                  30    
HELIX    9 AA9 LEU A  172  GLY A  190  1                                  19    
HELIX   10 AB1 ASP A  201  LYS A  208  1                                   8    
HELIX   11 AB2 LYS A  209  LYS A  212  5                                   4    
HELIX   12 AB3 ASP A  217  PHE A  226  1                                  10    
HELIX   13 AB4 PHE A  228  LEU A  236  1                                   9    
HELIX   14 AB5 PRO A  242  ASP A  263  1                                  22    
HELIX   15 AB6 ASP A  270  ASP A  277  1                                   8    
HELIX   16 AB7 SER A  278  SER A  281  5                                   4    
HELIX   17 AB8 SER A  291  HIS A  324  1                                  34    
HELIX   18 AB9 HIS A  324  LEU A  339  1                                  16    
HELIX   19 AC1 PRO A  340  ALA A  343  5                                   4    
HELIX   20 AC2 THR A  346  MET A  353  1                                   8    
HELIX   21 AC3 MET A  353  PHE A  367  1                                  15    
HELIX   22 AC4 PRO A  397  HIS A  403  1                                   7    
HELIX   23 AC5 ARG A  415  PHE A  419  5                                   5    
HELIX   24 AC6 GLY A  443  GLN A  460  1                                  18    
HELIX   25 AC7 GLY B   31  LEU B   36  1                                   6    
HELIX   26 AC8 ASN B   49  GLN B   55  5                                   7    
HELIX   27 AC9 GLY B   56  TYR B   68  1                                  13    
HELIX   28 AD1 ASP B   86  VAL B   95  1                                  10    
HELIX   29 AD2 VAL B  111  ALA B  117  5                                   7    
HELIX   30 AD3 GLU B  122  SER B  134  1                                  13    
HELIX   31 AD4 PRO B  135  PHE B  137  5                                   3    
HELIX   32 AD5 THR B  138  GLY B  167  1                                  30    
HELIX   33 AD6 LEU B  172  GLY B  190  1                                  19    
HELIX   34 AD7 ASP B  201  LYS B  208  1                                   8    
HELIX   35 AD8 LYS B  209  LYS B  212  5                                   4    
HELIX   36 AD9 ASP B  217  PHE B  226  1                                  10    
HELIX   37 AE1 LEU B  229  LEU B  236  1                                   8    
HELIX   38 AE2 PRO B  242  ASP B  263  1                                  22    
HELIX   39 AE3 ASP B  270  ASP B  277  1                                   8    
HELIX   40 AE4 SER B  278  ASN B  280  5                                   3    
HELIX   41 AE5 SER B  291  HIS B  324  1                                  34    
HELIX   42 AE6 HIS B  324  LEU B  339  1                                  16    
HELIX   43 AE7 THR B  346  VAL B  351  1                                   6    
HELIX   44 AE8 MET B  353  PHE B  367  1                                  15    
HELIX   45 AE9 PRO B  397  HIS B  403  1                                   7    
HELIX   46 AF1 ARG B  415  SER B  420  5                                   6    
HELIX   47 AF2 GLY B  443  GLN B  460  1                                  18    
HELIX   48 AF3 GLY C   31  LEU C   36  1                                   6    
HELIX   49 AF4 ASN C   49  GLN C   55  5                                   7    
HELIX   50 AF5 GLY C   56  TYR C   68  1                                  13    
HELIX   51 AF6 ASP C   86  VAL C   95  1                                  10    
HELIX   52 AF7 VAL C  111  ALA C  117  5                                   7    
HELIX   53 AF8 GLU C  122  SER C  134  1                                  13    
HELIX   54 AF9 PRO C  135  PHE C  137  5                                   3    
HELIX   55 AG1 THR C  138  LYS C  166  1                                  29    
HELIX   56 AG2 LEU C  172  GLY C  190  1                                  19    
HELIX   57 AG3 ASP C  194  ASN C  198  5                                   5    
HELIX   58 AG4 ASP C  201  LYS C  209  1                                   9    
HELIX   59 AG5 PHE C  210  PHE C  213  5                                   4    
HELIX   60 AG6 ASP C  217  PHE C  226  1                                  10    
HELIX   61 AG7 PHE C  228  LEU C  236  1                                   9    
HELIX   62 AG8 PRO C  242  SER C  259  1                                  18    
HELIX   63 AG9 ARG C  260  ASN C  262  5                                   3    
HELIX   64 AH1 ASP C  270  ASN C  280  1                                  11    
HELIX   65 AH2 SER C  291  HIS C  324  1                                  34    
HELIX   66 AH3 HIS C  324  LEU C  339  1                                  16    
HELIX   67 AH4 THR C  346  VAL C  351  1                                   6    
HELIX   68 AH5 MET C  353  PHE C  367  1                                  15    
HELIX   69 AH6 PRO C  397  HIS C  403  1                                   7    
HELIX   70 AH7 ARG C  415  SER C  420  5                                   6    
HELIX   71 AH8 GLY C  443  ASN C  461  1                                  19    
HELIX   72 AH9 GLY D   31  LEU D   36  1                                   6    
HELIX   73 AI1 ASN D   49  GLN D   55  5                                   7    
HELIX   74 AI2 GLY D   56  TYR D   68  1                                  13    
HELIX   75 AI3 ASP D   86  VAL D   95  1                                  10    
HELIX   76 AI4 VAL D  111  ALA D  117  5                                   7    
HELIX   77 AI5 GLU D  122  SER D  134  1                                  13    
HELIX   78 AI6 PRO D  135  PHE D  137  5                                   3    
HELIX   79 AI7 THR D  138  LYS D  166  1                                  29    
HELIX   80 AI8 LEU D  172  GLY D  190  1                                  19    
HELIX   81 AI9 ASP D  194  ASN D  198  5                                   5    
HELIX   82 AJ1 ASP D  201  LYS D  208  1                                   8    
HELIX   83 AJ2 ASP D  217  PHE D  226  1                                  10    
HELIX   84 AJ3 LEU D  229  LEU D  236  1                                   8    
HELIX   85 AJ4 PRO D  242  ASP D  263  1                                  22    
HELIX   86 AJ5 ASP D  270  ASP D  277  1                                   8    
HELIX   87 AJ6 SER D  278  ASN D  280  5                                   3    
HELIX   88 AJ7 SER D  291  HIS D  324  1                                  34    
HELIX   89 AJ8 HIS D  324  ALA D  337  1                                  14    
HELIX   90 AJ9 THR D  346  MET D  353  1                                   8    
HELIX   91 AK1 MET D  353  PHE D  367  1                                  15    
HELIX   92 AK2 PRO D  397  HIS D  403  1                                   7    
HELIX   93 AK3 ARG D  415  PHE D  419  5                                   5    
HELIX   94 AK4 GLY D  443  GLN D  460  1                                  18    
HELIX   95 AK5 GLY E   31  LEU E   36  1                                   6    
HELIX   96 AK6 ASN E   49  GLN E   55  5                                   7    
HELIX   97 AK7 GLY E   56  TYR E   68  1                                  13    
HELIX   98 AK8 ASP E   86  VAL E   95  1                                  10    
HELIX   99 AK9 LYS E   96  TYR E   99  5                                   4    
HELIX  100 AL1 VAL E  111  ALA E  121  5                                  11    
HELIX  101 AL2 GLU E  122  SER E  134  1                                  13    
HELIX  102 AL3 PRO E  135  PHE E  137  5                                   3    
HELIX  103 AL4 THR E  138  MET E  145  1                                   8    
HELIX  104 AL5 MET E  145  GLU E  165  1                                  21    
HELIX  105 AL6 LEU E  172  GLY E  190  1                                  19    
HELIX  106 AL7 ASP E  201  LYS E  208  1                                   8    
HELIX  107 AL8 ASP E  217  PHE E  226  1                                  10    
HELIX  108 AL9 LEU E  229  LEU E  236  1                                   8    
HELIX  109 AM1 PRO E  242  ASN E  262  1                                  21    
HELIX  110 AM2 ASP E  270  ASP E  277  1                                   8    
HELIX  111 AM3 SER E  291  HIS E  324  1                                  34    
HELIX  112 AM4 HIS E  324  LEU E  339  1                                  16    
HELIX  113 AM5 THR E  346  MET E  353  1                                   8    
HELIX  114 AM6 MET E  353  PHE E  367  1                                  15    
HELIX  115 AM7 PRO E  397  HIS E  403  1                                   7    
HELIX  116 AM8 ARG E  415  PHE E  419  5                                   5    
HELIX  117 AM9 GLY E  443  GLN E  460  1                                  18    
HELIX  118 AN1 GLY F   31  LEU F   36  1                                   6    
HELIX  119 AN2 ASN F   49  GLN F   55  5                                   7    
HELIX  120 AN3 GLY F   56  TYR F   68  1                                  13    
HELIX  121 AN4 ASP F   86  VAL F   95  1                                  10    
HELIX  122 AN5 VAL F  111  ALA F  117  5                                   7    
HELIX  123 AN6 GLU F  122  SER F  134  1                                  13    
HELIX  124 AN7 PRO F  135  PHE F  137  5                                   3    
HELIX  125 AN8 THR F  138  LYS F  166  1                                  29    
HELIX  126 AN9 LEU F  172  GLY F  190  1                                  19    
HELIX  127 AO1 ASP F  201  PHE F  213  1                                  13    
HELIX  128 AO2 ASP F  217  PHE F  226  1                                  10    
HELIX  129 AO3 LEU F  229  LEU F  236  1                                   8    
HELIX  130 AO4 PRO F  242  ASP F  263  1                                  22    
HELIX  131 AO5 ASP F  270  ASP F  277  1                                   8    
HELIX  132 AO6 SER F  278  ASN F  280  5                                   3    
HELIX  133 AO7 SER F  291  HIS F  324  1                                  34    
HELIX  134 AO8 HIS F  324  LEU F  339  1                                  16    
HELIX  135 AO9 THR F  346  VAL F  351  1                                   6    
HELIX  136 AP1 MET F  353  PHE F  367  1                                  15    
HELIX  137 AP2 PRO F  397  HIS F  403  1                                   7    
HELIX  138 AP3 ARG F  415  SER F  420  5                                   6    
HELIX  139 AP4 GLY F  443  GLN F  460  1                                  18    
HELIX  140 AP5 GLY G   31  GLY G   37  1                                   7    
HELIX  141 AP6 ASN G   49  GLN G   55  5                                   7    
HELIX  142 AP7 GLY G   56  TYR G   68  1                                  13    
HELIX  143 AP8 ASP G   86  VAL G   95  1                                  10    
HELIX  144 AP9 VAL G  111  ALA G  117  5                                   7    
HELIX  145 AQ1 GLU G  122  SER G  134  1                                  13    
HELIX  146 AQ2 PRO G  135  PHE G  137  5                                   3    
HELIX  147 AQ3 THR G  138  LYS G  166  1                                  29    
HELIX  148 AQ4 LEU G  172  PHE G  189  1                                  18    
HELIX  149 AQ5 ASP G  194  ASN G  198  5                                   5    
HELIX  150 AQ6 ASP G  201  LYS G  208  1                                   8    
HELIX  151 AQ7 ASP G  217  PHE G  226  1                                  10    
HELIX  152 AQ8 PHE G  228  LEU G  236  1                                   9    
HELIX  153 AQ9 PRO G  242  ASP G  263  1                                  22    
HELIX  154 AR1 ASP G  270  GLN G  279  1                                  10    
HELIX  155 AR2 SER G  291  THR G  323  1                                  33    
HELIX  156 AR3 HIS G  324  LEU G  339  1                                  16    
HELIX  157 AR4 THR G  346  MET G  353  1                                   8    
HELIX  158 AR5 MET G  353  PHE G  367  1                                  15    
HELIX  159 AR6 PRO G  397  HIS G  403  1                                   7    
HELIX  160 AR7 ARG G  415  PHE G  419  5                                   5    
HELIX  161 AR8 GLY G  443  ASN G  461  1                                  19    
HELIX  162 AR9 GLY H   31  GLY H   37  1                                   7    
HELIX  163 AS1 ASN H   49  GLN H   55  5                                   7    
HELIX  164 AS2 GLY H   56  TYR H   68  1                                  13    
HELIX  165 AS3 ASP H   86  VAL H   95  1                                  10    
HELIX  166 AS4 VAL H  111  ALA H  117  5                                   7    
HELIX  167 AS5 GLU H  122  SER H  134  1                                  13    
HELIX  168 AS6 PRO H  135  PHE H  137  5                                   3    
HELIX  169 AS7 THR H  138  LYS H  166  1                                  29    
HELIX  170 AS8 LEU H  172  GLY H  190  1                                  19    
HELIX  171 AS9 ASP H  201  LYS H  208  1                                   8    
HELIX  172 AT1 LYS H  209  LYS H  212  5                                   4    
HELIX  173 AT2 ASP H  217  PHE H  226  1                                  10    
HELIX  174 AT3 LEU H  229  LEU H  236  1                                   8    
HELIX  175 AT4 PRO H  242  ASN H  262  1                                  21    
HELIX  176 AT5 ASP H  270  ASN H  280  1                                  11    
HELIX  177 AT6 SER H  291  HIS H  324  1                                  34    
HELIX  178 AT7 HIS H  324  LEU H  339  1                                  16    
HELIX  179 AT8 THR H  346  MET H  353  1                                   8    
HELIX  180 AT9 MET H  353  PHE H  367  1                                  15    
HELIX  181 AU1 PRO H  397  HIS H  403  1                                   7    
HELIX  182 AU2 ARG H  415  PHE H  419  5                                   5    
HELIX  183 AU3 GLY H  443  GLN H  460  1                                  18    
HELIX  184 AU4 GLY I   31  LEU I   36  1                                   6    
HELIX  185 AU5 ASN I   49  ARG I   54  5                                   6    
HELIX  186 AU6 GLY I   56  TYR I   68  1                                  13    
HELIX  187 AU7 ASP I   86  VAL I   95  1                                  10    
HELIX  188 AU8 VAL I  111  ALA I  117  5                                   7    
HELIX  189 AU9 GLU I  122  SER I  134  1                                  13    
HELIX  190 AV1 PRO I  135  PHE I  137  5                                   3    
HELIX  191 AV2 THR I  138  LYS I  166  1                                  29    
HELIX  192 AV3 LEU I  172  GLY I  190  1                                  19    
HELIX  193 AV4 ASP I  194  ASN I  198  5                                   5    
HELIX  194 AV5 ASP I  201  LYS I  209  1                                   9    
HELIX  195 AV6 PHE I  210  PHE I  213  5                                   4    
HELIX  196 AV7 ASP I  217  PHE I  226  1                                  10    
HELIX  197 AV8 PHE I  228  LEU I  236  1                                   9    
HELIX  198 AV9 PRO I  242  SER I  259  1                                  18    
HELIX  199 AW1 ARG I  260  ASP I  263  5                                   4    
HELIX  200 AW2 ASP I  270  ASN I  280  1                                  11    
HELIX  201 AW3 SER I  291  HIS I  324  1                                  34    
HELIX  202 AW4 HIS I  324  LEU I  339  1                                  16    
HELIX  203 AW5 THR I  346  VAL I  351  1                                   6    
HELIX  204 AW6 MET I  353  PHE I  367  1                                  15    
HELIX  205 AW7 PRO I  397  HIS I  403  1                                   7    
HELIX  206 AW8 ARG I  415  PHE I  419  5                                   5    
HELIX  207 AW9 GLY I  443  GLN I  460  1                                  18    
HELIX  208 AX1 GLY J   31  GLY J   37  1                                   7    
HELIX  209 AX2 ASN J   49  GLN J   55  5                                   7    
HELIX  210 AX3 GLY J   56  TYR J   68  1                                  13    
HELIX  211 AX4 ASP J   86  VAL J   95  1                                  10    
HELIX  212 AX5 VAL J  111  ALA J  117  5                                   7    
HELIX  213 AX6 GLU J  122  SER J  134  1                                  13    
HELIX  214 AX7 PRO J  135  PHE J  137  5                                   3    
HELIX  215 AX8 THR J  138  MET J  145  1                                   8    
HELIX  216 AX9 MET J  145  LYS J  166  1                                  22    
HELIX  217 AY1 LEU J  172  GLY J  190  1                                  19    
HELIX  218 AY2 ASP J  194  ASN J  198  5                                   5    
HELIX  219 AY3 ASP J  201  LYS J  208  1                                   8    
HELIX  220 AY4 LYS J  209  LEU J  211  5                                   3    
HELIX  221 AY5 ASP J  217  PHE J  226  1                                  10    
HELIX  222 AY6 LEU J  229  LEU J  236  1                                   8    
HELIX  223 AY7 PRO J  242  ASN J  262  1                                  21    
HELIX  224 AY8 ASP J  270  GLN J  279  1                                  10    
HELIX  225 AY9 SER J  291  HIS J  324  1                                  34    
HELIX  226 AZ1 HIS J  324  LEU J  339  1                                  16    
HELIX  227 AZ2 THR J  346  VAL J  351  1                                   6    
HELIX  228 AZ3 MET J  353  PHE J  367  1                                  15    
HELIX  229 AZ4 PRO J  397  HIS J  403  1                                   7    
HELIX  230 AZ5 ARG J  415  SER J  420  5                                   6    
HELIX  231 AZ6 GLY J  443  GLN J  460  1                                  18    
HELIX  232 AZ7 GLY K   31  GLY K   37  1                                   7    
HELIX  233 AZ8 ASN K   49  ARG K   54  5                                   6    
HELIX  234 AZ9 GLY K   56  TYR K   68  1                                  13    
HELIX  235 BA1 ASP K   86  VAL K   95  1                                  10    
HELIX  236 BA2 VAL K  111  ALA K  117  5                                   7    
HELIX  237 BA3 GLU K  122  SER K  134  1                                  13    
HELIX  238 BA4 PRO K  135  PHE K  137  5                                   3    
HELIX  239 BA5 THR K  138  LYS K  166  1                                  29    
HELIX  240 BA6 LEU K  172  GLY K  190  1                                  19    
HELIX  241 BA7 ASP K  194  ASN K  198  5                                   5    
HELIX  242 BA8 ASP K  201  LYS K  208  1                                   8    
HELIX  243 BA9 LYS K  209  LYS K  212  5                                   4    
HELIX  244 BB1 ASP K  217  PHE K  226  1                                  10    
HELIX  245 BB2 LEU K  229  LEU K  236  1                                   8    
HELIX  246 BB3 PRO K  242  ASP K  263  1                                  22    
HELIX  247 BB4 ASP K  270  ASP K  277  1                                   8    
HELIX  248 BB5 SER K  278  ASN K  280  5                                   3    
HELIX  249 BB6 SER K  291  THR K  323  1                                  33    
HELIX  250 BB7 HIS K  324  LEU K  339  1                                  16    
HELIX  251 BB8 THR K  346  MET K  353  1                                   8    
HELIX  252 BB9 MET K  353  PHE K  367  1                                  15    
HELIX  253 BC1 PRO K  397  HIS K  403  1                                   7    
HELIX  254 BC2 ARG K  415  PHE K  419  5                                   5    
HELIX  255 BC3 GLY K  443  GLN K  460  1                                  18    
HELIX  256 BC4 GLY L   31  GLY L   37  1                                   7    
HELIX  257 BC5 ASN L   49  ARG L   54  5                                   6    
HELIX  258 BC6 GLY L   56  TYR L   68  1                                  13    
HELIX  259 BC7 ASP L   86  VAL L   95  1                                  10    
HELIX  260 BC8 VAL L  111  ALA L  117  5                                   7    
HELIX  261 BC9 GLU L  122  SER L  134  1                                  13    
HELIX  262 BD1 PRO L  135  PHE L  137  5                                   3    
HELIX  263 BD2 THR L  138  GLY L  167  1                                  30    
HELIX  264 BD3 LEU L  172  GLY L  190  1                                  19    
HELIX  265 BD4 ASP L  201  LYS L  209  1                                   9    
HELIX  266 BD5 PHE L  210  LYS L  212  5                                   3    
HELIX  267 BD6 ASP L  217  PHE L  226  1                                  10    
HELIX  268 BD7 LEU L  229  LEU L  236  1                                   8    
HELIX  269 BD8 PRO L  242  ASN L  262  1                                  21    
HELIX  270 BD9 LEU L  272  ASP L  277  1                                   6    
HELIX  271 BE1 SER L  278  ASN L  280  5                                   3    
HELIX  272 BE2 SER L  291  HIS L  324  1                                  34    
HELIX  273 BE3 HIS L  324  LEU L  339  1                                  16    
HELIX  274 BE4 PRO L  340  ALA L  343  5                                   4    
HELIX  275 BE5 THR L  346  MET L  353  1                                   8    
HELIX  276 BE6 MET L  353  PHE L  367  1                                  15    
HELIX  277 BE7 PRO L  397  HIS L  403  1                                   7    
HELIX  278 BE8 ARG L  415  SER L  420  5                                   6    
HELIX  279 BE9 GLY L  443  GLN L  460  1                                  18    
SHEET    1 AA1 4 MET A  71  GLU A  76  0                                        
SHEET    2 AA1 4 LEU A  79  ILE A  84 -1  O  ALA A  83   N  TRP A  72           
SHEET    3 AA1 4 MET A 393  ILE A 396  1  O  VAL A 395   N  LEU A  82           
SHEET    4 AA1 4 LEU A 373  THR A 376 -1  N  ARG A 375   O  VAL A 394           
SHEET    1 AA2 3 VAL A 170  THR A 171  0                                        
SHEET    2 AA2 3 VAL A 489  SER A 494 -1  O  LEU A 490   N  VAL A 170           
SHEET    3 AA2 3 PHE A 462  LYS A 465 -1  N  LYS A 465   O  LYS A 491           
SHEET    1 AA3 2 VAL A 381  GLU A 382  0                                        
SHEET    2 AA3 2 PHE A 387  ILE A 388 -1  O  ILE A 388   N  VAL A 381           
SHEET    1 AA4 4 TRP B  72  GLU B  76  0                                        
SHEET    2 AA4 4 LEU B  79  ALA B  83 -1  O  VAL B  81   N  THR B  74           
SHEET    3 AA4 4 MET B 393  ILE B 396  1  O  VAL B 395   N  LEU B  82           
SHEET    4 AA4 4 LEU B 373  THR B 376 -1  N  LEU B 373   O  ILE B 396           
SHEET    1 AA5 3 VAL B 170  THR B 171  0                                        
SHEET    2 AA5 3 VAL B 489  SER B 494 -1  O  LEU B 490   N  VAL B 170           
SHEET    3 AA5 3 PHE B 462  LYS B 465 -1  N  LYS B 465   O  LYS B 491           
SHEET    1 AA6 2 VAL B 381  GLU B 382  0                                        
SHEET    2 AA6 2 PHE B 387  ILE B 388 -1  O  ILE B 388   N  VAL B 381           
SHEET    1 AA7 4 MET C  71  GLU C  76  0                                        
SHEET    2 AA7 4 LEU C  79  ILE C  84 -1  O  ALA C  83   N  TRP C  72           
SHEET    3 AA7 4 MET C 393  ILE C 396  1  O  MET C 393   N  LEU C  82           
SHEET    4 AA7 4 LEU C 373  THR C 376 -1  N  ARG C 375   O  VAL C 394           
SHEET    1 AA8 3 VAL C 170  THR C 171  0                                        
SHEET    2 AA8 3 VAL C 489  SER C 494 -1  O  LEU C 490   N  VAL C 170           
SHEET    3 AA8 3 PHE C 462  PRO C 466 -1  N  LYS C 465   O  LYS C 491           
SHEET    1 AA9 2 VAL C 381  ILE C 383  0                                        
SHEET    2 AA9 2 VAL C 386  ILE C 388 -1  O  VAL C 386   N  ILE C 383           
SHEET    1 AB1 4 MET D  71  GLU D  76  0                                        
SHEET    2 AB1 4 LEU D  79  ILE D  84 -1  O  VAL D  81   N  THR D  74           
SHEET    3 AB1 4 MET D 393  ILE D 396  1  O  MET D 393   N  LEU D  82           
SHEET    4 AB1 4 LEU D 373  THR D 376 -1  N  ARG D 375   O  VAL D 394           
SHEET    1 AB2 3 VAL D 170  THR D 171  0                                        
SHEET    2 AB2 3 VAL D 489  SER D 494 -1  O  LEU D 490   N  VAL D 170           
SHEET    3 AB2 3 PHE D 462  PRO D 466 -1  N  LYS D 465   O  LYS D 491           
SHEET    1 AB3 2 VAL D 381  ILE D 383  0                                        
SHEET    2 AB3 2 VAL D 386  ILE D 388 -1  O  ILE D 388   N  VAL D 381           
SHEET    1 AB4 4 MET E  71  GLU E  76  0                                        
SHEET    2 AB4 4 LEU E  79  ILE E  84 -1  O  VAL E  81   N  THR E  74           
SHEET    3 AB4 4 MET E 393  ILE E 396  1  O  VAL E 395   N  LEU E  82           
SHEET    4 AB4 4 LEU E 373  THR E 376 -1  N  ARG E 375   O  VAL E 394           
SHEET    1 AB5 2 VAL E 170  THR E 171  0                                        
SHEET    2 AB5 2 VAL E 489  LEU E 490 -1  O  LEU E 490   N  VAL E 170           
SHEET    1 AB6 2 VAL E 381  ILE E 383  0                                        
SHEET    2 AB6 2 VAL E 386  ILE E 388 -1  O  ILE E 388   N  VAL E 381           
SHEET    1 AB7 4 TRP F  72  GLU F  76  0                                        
SHEET    2 AB7 4 LEU F  79  ALA F  83 -1  O  VAL F  81   N  THR F  74           
SHEET    3 AB7 4 MET F 393  ILE F 396  1  O  VAL F 395   N  LEU F  82           
SHEET    4 AB7 4 LEU F 373  THR F 376 -1  N  ARG F 375   O  VAL F 394           
SHEET    1 AB8 3 VAL F 170  THR F 171  0                                        
SHEET    2 AB8 3 VAL F 489  SER F 494 -1  O  LEU F 490   N  VAL F 170           
SHEET    3 AB8 3 PHE F 462  PRO F 466 -1  N  LYS F 465   O  LYS F 491           
SHEET    1 AB9 2 VAL F 381  ILE F 383  0                                        
SHEET    2 AB9 2 VAL F 386  ILE F 388 -1  O  ILE F 388   N  VAL F 381           
SHEET    1 AC1 4 MET G  71  GLU G  76  0                                        
SHEET    2 AC1 4 LEU G  79  ILE G  84 -1  O  VAL G  81   N  THR G  74           
SHEET    3 AC1 4 MET G 393  ILE G 396  1  O  MET G 393   N  LEU G  82           
SHEET    4 AC1 4 LEU G 373  THR G 376 -1  N  ARG G 375   O  VAL G 394           
SHEET    1 AC2 3 VAL G 170  THR G 171  0                                        
SHEET    2 AC2 3 VAL G 489  SER G 494 -1  O  LEU G 490   N  VAL G 170           
SHEET    3 AC2 3 PHE G 462  LYS G 465 -1  N  LYS G 465   O  LYS G 491           
SHEET    1 AC3 2 VAL G 381  ILE G 383  0                                        
SHEET    2 AC3 2 VAL G 386  ILE G 388 -1  O  ILE G 388   N  VAL G 381           
SHEET    1 AC4 4 MET H  71  GLU H  76  0                                        
SHEET    2 AC4 4 LEU H  79  ILE H  84 -1  O  VAL H  81   N  THR H  74           
SHEET    3 AC4 4 MET H 393  ILE H 396  1  O  VAL H 395   N  LEU H  82           
SHEET    4 AC4 4 LEU H 373  THR H 376 -1  N  ARG H 375   O  VAL H 394           
SHEET    1 AC5 3 VAL H 170  THR H 171  0                                        
SHEET    2 AC5 3 VAL H 489  SER H 494 -1  O  LEU H 490   N  VAL H 170           
SHEET    3 AC5 3 PHE H 462  LYS H 465 -1  N  LYS H 465   O  LYS H 491           
SHEET    1 AC6 2 VAL H 381  ILE H 383  0                                        
SHEET    2 AC6 2 VAL H 386  ILE H 388 -1  O  VAL H 386   N  ILE H 383           
SHEET    1 AC7 4 MET I  71  GLU I  76  0                                        
SHEET    2 AC7 4 LEU I  79  ILE I  84 -1  O  VAL I  81   N  THR I  74           
SHEET    3 AC7 4 MET I 393  ILE I 396  1  O  VAL I 395   N  LEU I  82           
SHEET    4 AC7 4 LEU I 373  THR I 376 -1  N  ARG I 375   O  VAL I 394           
SHEET    1 AC8 3 VAL I 170  THR I 171  0                                        
SHEET    2 AC8 3 VAL I 489  SER I 494 -1  O  LEU I 490   N  VAL I 170           
SHEET    3 AC8 3 PHE I 462  LYS I 465 -1  N  LYS I 465   O  LYS I 491           
SHEET    1 AC9 2 VAL I 381  ILE I 383  0                                        
SHEET    2 AC9 2 VAL I 386  ILE I 388 -1  O  VAL I 386   N  ILE I 383           
SHEET    1 AD1 4 MET J  71  GLU J  76  0                                        
SHEET    2 AD1 4 LEU J  79  ILE J  84 -1  O  VAL J  81   N  THR J  74           
SHEET    3 AD1 4 MET J 393  ILE J 396  1  O  MET J 393   N  LEU J  82           
SHEET    4 AD1 4 LEU J 373  THR J 376 -1  N  LEU J 373   O  ILE J 396           
SHEET    1 AD2 3 VAL J 170  THR J 171  0                                        
SHEET    2 AD2 3 VAL J 489  SER J 494 -1  O  LEU J 490   N  VAL J 170           
SHEET    3 AD2 3 PHE J 462  LYS J 465 -1  N  LYS J 465   O  LYS J 491           
SHEET    1 AD3 2 VAL J 381  ILE J 383  0                                        
SHEET    2 AD3 2 VAL J 386  ILE J 388 -1  O  ILE J 388   N  VAL J 381           
SHEET    1 AD4 4 MET K  71  GLU K  76  0                                        
SHEET    2 AD4 4 LEU K  79  ILE K  84 -1  O  VAL K  81   N  THR K  74           
SHEET    3 AD4 4 MET K 393  ILE K 396  1  O  VAL K 395   N  LEU K  82           
SHEET    4 AD4 4 LEU K 373  THR K 376 -1  N  LEU K 373   O  ILE K 396           
SHEET    1 AD5 3 VAL K 170  THR K 171  0                                        
SHEET    2 AD5 3 VAL K 489  SER K 494 -1  O  LEU K 490   N  VAL K 170           
SHEET    3 AD5 3 PHE K 462  LYS K 465 -1  N  LYS K 465   O  LYS K 491           
SHEET    1 AD6 2 VAL K 381  GLU K 382  0                                        
SHEET    2 AD6 2 PHE K 387  ILE K 388 -1  O  ILE K 388   N  VAL K 381           
SHEET    1 AD7 4 MET L  71  GLU L  76  0                                        
SHEET    2 AD7 4 LEU L  79  ILE L  84 -1  O  VAL L  81   N  THR L  74           
SHEET    3 AD7 4 MET L 393  ILE L 396  1  O  VAL L 395   N  LEU L  82           
SHEET    4 AD7 4 LEU L 373  THR L 376 -1  N  LEU L 373   O  ILE L 396           
SHEET    1 AD8 3 VAL L 170  THR L 171  0                                        
SHEET    2 AD8 3 VAL L 489  ASP L 493 -1  O  LEU L 490   N  VAL L 170           
SHEET    3 AD8 3 SER L 463  LYS L 465 -1  N  SER L 463   O  ASP L 493           
SHEET    1 AD9 2 VAL L 381  GLU L 382  0                                        
SHEET    2 AD9 2 PHE L 387  ILE L 388 -1  O  ILE L 388   N  VAL L 381           
LINK         SG  CYS A 441                FE   HEM A 601     1555   1555  2.25  
LINK         SG  CYS B 441                FE   HEM B 601     1555   1555  2.25  
LINK         SG  CYS C 441                FE   HEM C 601     1555   1555  2.26  
LINK         SG  CYS D 441                FE   HEM D 601     1555   1555  2.25  
LINK         SG  CYS E 441                FE   HEM E 601     1555   1555  2.24  
LINK         SG  CYS F 441                FE   HEM F 601     1555   1555  2.25  
LINK         SG  CYS G 441                FE   HEM G 601     1555   1555  2.25  
LINK         SG  CYS H 441                FE   HEM H 601     1555   1555  2.26  
LINK         SG  CYS I 441                FE   HEM I 601     1555   1555  2.26  
LINK         SG  CYS J 441                FE   HEM J 601     1555   1555  2.26  
LINK         SG  CYS K 441                FE   HEM K 601     1555   1555  2.26  
LINK         SG  CYS L 441                FE   HEM L 601     1555   1555  2.26  
LINK        FE   HEM A 601                 N5  RIT A 602     1555   1555  2.20  
LINK        FE   HEM B 601                 N5  RIT B 602     1555   1555  2.16  
LINK        FE   HEM H 601                 N5  RIT H 602     1555   1555  2.27  
CISPEP   1 ILE A  472    PRO A  473          0        -1.38                     
CISPEP   2 ILE B  472    PRO B  473          0        -0.66                     
CISPEP   3 ILE C  472    PRO C  473          0        -1.33                     
CISPEP   4 ILE D  472    PRO D  473          0        -1.06                     
CISPEP   5 ILE E  472    PRO E  473          0        -1.67                     
CISPEP   6 ILE F  472    PRO F  473          0        -2.02                     
CISPEP   7 ILE G  472    PRO G  473          0        -2.18                     
CISPEP   8 ILE H  472    PRO H  473          0        -2.44                     
CISPEP   9 ILE I  472    PRO I  473          0        -2.03                     
CISPEP  10 ILE J  472    PRO J  473          0        -1.51                     
CISPEP  11 ILE K  472    PRO K  473          0        -0.83                     
CISPEP  12 ILE L  472    PRO L  473          0        -1.81                     
SITE     1 AC1 17 ARG A 105  ILE A 118  TRP A 126  ARG A 130                    
SITE     2 AC1 17 PHE A 302  ALA A 305  THR A 309  VAL A 313                    
SITE     3 AC1 17 ARG A 375  PRO A 433  PHE A 434  GLY A 435                    
SITE     4 AC1 17 ARG A 439  CYS A 441  ILE A 442  ALA A 447                    
SITE     5 AC1 17 RIT A 602                                                     
SITE     1 AC2 11 SER A 119  LEU A 120  PHE A 210  PHE A 213                    
SITE     2 AC2 11 PHE A 215  PHE A 220  PHE A 241  PHE A 304                    
SITE     3 AC2 11 THR A 309  ALA A 370  HEM A 601                               
SITE     1 AC3 18 ARG B 105  ILE B 118  TRP B 126  ARG B 130                    
SITE     2 AC3 18 PHE B 302  ALA B 305  THR B 309  VAL B 369                    
SITE     3 AC3 18 LEU B 373  ARG B 375  PRO B 433  PHE B 434                    
SITE     4 AC3 18 ARG B 439  ASN B 440  CYS B 441  ILE B 442                    
SITE     5 AC3 18 ALA B 447  RIT B 602                                          
SITE     1 AC4 12 ARG B 106  LEU B 120  PHE B 210  PHE B 215                    
SITE     2 AC4 12 PHE B 241  ILE B 301  PHE B 304  ALA B 370                    
SITE     3 AC4 12 ILE B 371  GLU B 374  GLY B 480  HEM B 601                    
SITE     1 AC5 17 ARG C 105  ILE C 118  TRP C 126  ARG C 130                    
SITE     2 AC5 17 PHE C 302  ALA C 305  THR C 309  VAL C 313                    
SITE     3 AC5 17 ALA C 370  ARG C 375  PRO C 433  PHE C 434                    
SITE     4 AC5 17 ARG C 439  ASN C 440  CYS C 441  ILE C 442                    
SITE     5 AC5 17 ALA C 447                                                     
SITE     1 AC6 18 ARG D 105  ILE D 118  SER D 119  TRP D 126                    
SITE     2 AC6 18 ARG D 130  PHE D 302  ALA D 305  THR D 309                    
SITE     3 AC6 18 VAL D 313  LEU D 373  ARG D 375  PRO D 433                    
SITE     4 AC6 18 PHE D 434  ARG D 439  CYS D 441  ILE D 442                    
SITE     5 AC6 18 PHE D 446  ALA D 447                                          
SITE     1 AC7 17 ARG E 105  ILE E 118  TRP E 126  ARG E 130                    
SITE     2 AC7 17 PHE E 302  ALA E 305  THR E 309  VAL E 313                    
SITE     3 AC7 17 ALA E 370  LEU E 373  ARG E 375  PRO E 433                    
SITE     4 AC7 17 PHE E 434  ARG E 439  CYS E 441  ILE E 442                    
SITE     5 AC7 17 MET E 451                                                     
SITE     1 AC8 16 ARG F 105  ILE F 118  TRP F 126  ARG F 130                    
SITE     2 AC8 16 PHE F 302  ALA F 305  GLY F 306  THR F 309                    
SITE     3 AC8 16 VAL F 313  ARG F 375  PRO F 433  PHE F 434                    
SITE     4 AC8 16 ARG F 439  CYS F 441  ILE F 442  ALA F 447                    
SITE     1 AC9 17 ARG G 105  ILE G 118  TRP G 126  ARG G 130                    
SITE     2 AC9 17 PHE G 302  ALA G 305  THR G 309  VAL G 313                    
SITE     3 AC9 17 ARG G 375  PRO G 433  PHE G 434  GLY G 435                    
SITE     4 AC9 17 ARG G 439  ASN G 440  CYS G 441  ILE G 442                    
SITE     5 AC9 17 ALA G 447                                                     
SITE     1 AD1 17 ARG H 105  ILE H 118  TRP H 126  ARG H 130                    
SITE     2 AD1 17 PHE H 302  ALA H 305  THR H 309  VAL H 369                    
SITE     3 AD1 17 LEU H 373  ARG H 375  PRO H 433  PHE H 434                    
SITE     4 AD1 17 ARG H 439  CYS H 441  ILE H 442  ALA H 447                    
SITE     5 AD1 17 RIT H 602                                                     
SITE     1 AD2 15 ARG H 105  ARG H 106  LEU H 120  PHE H 213                    
SITE     2 AD2 15 GLY H 214  PHE H 220  LEU H 240  ILE H 301                    
SITE     3 AD2 15 PHE H 304  ALA H 305  THR H 309  GLU H 374                    
SITE     4 AD2 15 GLY H 480  LEU H 481  HEM H 601                               
SITE     1 AD3 18 ARG I 105  ILE I 118  TRP I 126  ARG I 130                    
SITE     2 AD3 18 PHE I 302  ALA I 305  GLY I 306  THR I 309                    
SITE     3 AD3 18 VAL I 313  ALA I 370  ARG I 375  PRO I 433                    
SITE     4 AD3 18 PHE I 434  ARG I 439  ASN I 440  CYS I 441                    
SITE     5 AD3 18 ILE I 442  ALA I 447                                          
SITE     1 AD4 18 ARG J 105  ILE J 118  TRP J 126  ARG J 130                    
SITE     2 AD4 18 ALA J 305  THR J 309  VAL J 313  ALA J 370                    
SITE     3 AD4 18 LEU J 373  ARG J 375  PRO J 433  PHE J 434                    
SITE     4 AD4 18 GLY J 435  ARG J 439  ASN J 440  CYS J 441                    
SITE     5 AD4 18 ILE J 442  ALA J 447                                          
SITE     1 AD5 19 ARG K 105  ILE K 118  TRP K 126  ARG K 130                    
SITE     2 AD5 19 PHE K 302  ALA K 305  THR K 309  VAL K 313                    
SITE     3 AD5 19 VAL K 369  LEU K 373  ARG K 375  PRO K 433                    
SITE     4 AD5 19 PHE K 434  GLY K 435  ARG K 439  ASN K 440                    
SITE     5 AD5 19 CYS K 441  ILE K 442  ALA K 447                               
SITE     1 AD6 18 ARG L 105  ILE L 118  SER L 119  TRP L 126                    
SITE     2 AD6 18 ARG L 130  ILE L 184  PHE L 302  ALA L 305                    
SITE     3 AD6 18 THR L 309  ALA L 370  LEU L 373  ARG L 375                    
SITE     4 AD6 18 PRO L 433  PHE L 434  ARG L 439  ASN L 440                    
SITE     5 AD6 18 CYS L 441  ALA L 447                                          
CRYST1  148.988  198.384  234.881  90.00  90.00  90.00 P 21 21 21   48          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006712  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005041  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004257        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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